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[Entries: 476] New Search
1.
A. Bax: Two Dimensional Nuclear Magnetic Resonance in Liquids. PhD dissertation. Reidel, Boston, 1982.(1.pdf, 6582736 Bytes)
2.
S. Emid, A. Bax, J. Konijnendijk, J. Smidt and A. Pines: Multiple quantum coherence in dipolar relaxation measurements. Physica 96B, 333-336 (1979). (2.pdf, 288227 Bytes)(DOI)
3.
A. Bax, A.F. Mehlkopf and J. Smidt: Absorption spectra from phase-modulated spin echoes. J. Magn. Reson. 35, 373-378 (1979). (3.pdf, 241270 Bytes)(DOI)
4.
A. Bax, P.G. de Jong, A.F. Mehlkopf and J. Smidt: Separation of the different orders of multiple quantum transitions by the use of pulsed field gradients. Chem. Phys. Lett. 69, 567-570 (1980). (4.pdf, 322691 Bytes)(DOI)
5.
A. Bax and R. Freeman: Enhanced NMR resolution by restricting the effective sample volume. J. Magn. Reson. 37, 177-181 (1980). (5.pdf, 298189 Bytes)(DOI)
6.
A. Bax, A.F. Mehlkopf and J. Smidt: A fast method for obtaining 2D J-resolved absorption spectra. J. Magn. Reson. 40, 213-219 (1980). (6.pdf, 1446576 Bytes)(DOI)
7.
A. Bax, S.P. Kempsell and R. Freeman: Natural abundance 13C-13C coupling observed via double quantum coherence. J. Am. Chem. Soc. 102, 4849-4851 (1980). (7.pdf, 411195 Bytes)(DOI)
8.
A. Bax, S.P. Kempsell and R. Freeman: Investigation of long-range 13C-13C coupling in natural abundance samples. J. Magn. Reson. 41, 349-353 (1980). (8.pdf, 293306 Bytes)(DOI)
9.
A. Bax, A.F. Mehlkopf, J. Smidt and R. Freeman: A simple method for detection of zero-quantum transitions in NMR. J. Magn. Reson. 41, 502-506 (1980). (9.pdf, 321829 Bytes)(DOI)
10.
A. Bax and R. Freeman: Investigation of 13C-13C coupling in natural abundance samples: The strong coupling case. J. Magn. Reson. 41, 507-511 (1980). (10.pdf, 280143 Bytes)(DOI)
11.
A. Bax, R. Freeman and G.A. Morris: Correlation of proton chemical shifts by two-dimensional Fourier transform NMR. J. Magn. Reson. 42, 164-168 (1981). (11.pdf, 399949 Bytes)(DOI)
12.
A. Bax and G.A. Morris: An improved method for heteronuclear chemical shift correlation by two-dimensional NMR. J. Magn. Reson. 42, 501-505 (1981). (12.pdf, 637321 Bytes)(DOI)
13.
A. Bax, R. Freeman and G.A. Morris: A simple method for suppressing dispersion-mode contributions in NMR spectra: The "pseudo echo." J. Magn. Reson. 43, 333-338 (1981). (13.pdf, 373241 Bytes)(DOI)
14.
A. Bax, T.A. Frenkiel and R. Freeman: A NMR technique for tracing out the carbon skeleton of an organic molecule. J. Am. Chem. Soc. 103, 2102-2104 (1981). (14.pdf, 403518 Bytes)(DOI)
15.
A. Bax, R. Freeman, T.A. Frenkiel and M.H. Levitt: Assignment of carbon-13 NMR spectra via double quantum coherence. J. Magn. Reson. 43, 478-483 (1981). (15.pdf, 350330 Bytes)(DOI)
16.
A. Bax and R. Freeman: Investigation of complex networks of spin-spin coupling by two-dimensional NMR. J. Magn. Reson. 44, 542-561 (1981). (16.pdf, 2133161 Bytes)(DOI)
17.
A. Bax and R. Freeman: Relative signs of NMR spin coupling constants by two-dimensional Fourier transform spectroscopy. J. Magn. Reson. 45, 177-181 (1981). (17.pdf, 306075 Bytes)(DOI)
18.
A. Bax, A. F. Mehlkopf and J. Smidt: Homonuclear broad-band decoupled absorption spectra. J. Magn. Reson. 35, 167-169 (1979). (18.pdf, 141145 Bytes)(DOI)
19.
A. Bax and R. Freeman: Long-range proton-carbon-13 NMR spin coupling constants. J. Am. Chem. Soc. 104, 1099-1100 (1982). (19.pdf, 269233 Bytes)(DOI)
20.
A. Bax, N.M. Szeverenyi and G.E. Maciel: Pulsed polarization transfer for 13C NMR in solids. J. Magn. Reson. 50, 227-232 (1982). (20.pdf, 418881 Bytes)(DOI)
21.
A. Bax: Two-dimensional nuclear magnetic resonance spectroscopy. Proc. of the Eighth in the Series of USDA Science Symposia, 1982, 254-269.
22.
A. Bax, N.M. Szeverenyi and G.E. Maciel: Chemical shift anisotropy in powdered solids studied by 2D FT CP/MAS NMR. J. Magn. Reson. 51, 400-408 (1983). (22.pdf, 586274 Bytes)(DOI)
23.
A. Bax, T.A. Early and G.E. Maciel: Proton chemical shifts in polycrystalline solids determined by off-resonance decoupling. J. Magn. Reson. 52, 35-41 (1983). (23.pdf, 643722 Bytes)(DOI)
24.
N.M. Szeverenyi, A.Bax and G.E. Maciel: Proton exchange rates in solid tropolone as measured via 13C CP/MAS NMR. J. Am. Chem. Soc. 105, 2579-2582 (1983). (24.pdf, 478428 Bytes)(DOI)
25.
A. Bax: A simple method for the calibration of the decoupler radio-frequency field strength. J. Magn. Reson. 52, 76-80 (1983). (25.pdf, 271219 Bytes)(DOI)
26.
A. Bax, N.M. Szeverenyi and G.E. Maciel: Correlation of isotropic shifts and chemical shift anisotropy by two-dimensional Fourier transform magic angle hopping spectroscopy. J. Magn. Reson. 52, 147-152 (1983). (26.pdf, 532840 Bytes)(DOI)
27.
A. Bax: Determination of heteronuclear coupling constants via semi-selective two-dimensional J spectroscopy. J. Magn. Reson. 52, 330-334 (1983). (27.pdf, 317043 Bytes)(DOI)
28.
A. Bax: Two-dimensional heteronuclear relayed coherence transfer spectroscopy. J. Magn. Reson. 53, 149-153 (1983). (28.pdf, 341620 Bytes)(DOI)
29.
A.F. Mehlkopf, A. Bax, J. Smidt and T.A. Tiggelman: Design, control system and software organization of multi-purpose NMR spectrometers. I: The basis requirements and overall design. Computer Enhanced Spectroscopy 1, 3-10 (1983). (29.pdf, scanned, 174471 Bytes)
30.
A. Bax and T.H. Mareci: Practical aspects of carbon-l3 double quantum NMR. J. Magn. Reson. 53, 360-363 (1983). (30.pdf, 288114 Bytes)(DOI)
31.
A. Bax: Broadband homonuclear decoupling in heteronuclear shift correlation NMR spectroscopy. J. Magn. Reson. 53, 517-520 (1983). (31.pdf, 243561 Bytes)(DOI)
32.
A. Bax, R.H. Griffey and B.L. Hawkins: Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 55, 301-315 (1983). (32.pdf, 916448 Bytes)(DOI)
33.
A. Bax, N.M. Szeverenyi and G.E. Maciel: Chemical shift anisotropy in powdered solids studied by 2D FT NMR with flipping of the spinning axis. J. Magn. Reson. 55, 494-497 (1983). (33.pdf, 217456 Bytes)(DOI)
34.
R.H. Griffey, C.D. Poulter, A. Bax, B.L. Hawkins, Z. Yamaizuimi and S. Mishimura: Multiple quantum two-dimensional 1H-15N nuclear magnetic resonance spectroscopy: Chemical shift correlation maps of exchangeable imino protons of Escherichia coli tRNAfMet in water. Proc. Natl. Acad. Sci. USA 80, 5895-5897 (1983). (34.pdf, 564044 Bytes)(DOI)(pubmed)
35.
A. Bax, R.H. Griffey and B.L. Hawkins: Sensitivity-enhanced correlation of 15N and 1H chemical shifts in natural-abundance samples via multiple quantum coherence. J. Am. Chem. Soc. 105, 7188-7190 (1983). (35.pdf, 454800 Bytes)(DOI)
36.
A. Bax, N.M. Szeverenyi and G.E. Maciel: Two-dimensional NMR spectroscopy. In "Magnetic Resonance: Introduction, Advanced Topics and Application to Fossil Energy," L. Petrakis and J.P. Fraissard, (Eds.), Reidel, Dordrecht, 1984, pp. 137-148. (36.pdf, scanned, 543926 Bytes)
37.
T.A. Early, J.F. Haw, A. Bax and G.E. Maciel: 13C NMR studies of a solid inclusion complex. J. Phys. Chem. 88, 324-327 (1984). (37.pdf, 501634 Bytes)(DOI)
38.
A. Bax: Two-dimensional 13C NMR spectroscopy. In "Topics in 13C NMR Spectroscopy," G.C. Levy, (Ed.), Wiley Interscience, New York, 1984, pp. 197-238. (38.pdf, scanned, 624566 Bytes)
39.
A. Bax, C.H. Niu and D. Live: Sensitivity-enhanced NMR detection of nonprotonated 15N nuclei. J. Am. Chem. Soc. 106, 1150-1151 (1984). (39.pdf, 315334 Bytes)(DOI)
40.
A. Bax: Structure determination and spectral assignment by pulsed polarization transfer via long-range 1H-13C couplings. J. Magn. Reson. 57, 314-318 (1984). (40.pdf, 358512 Bytes)(DOI)
41.
J.S. Cohen, C. Chen and A. Bax: Selective observation of phosphate ester protons by 1H (31P) spin echo difference spectroscopy. J. Magn. Reson. 59, 181-187 (1984). (41.pdf, 325169 Bytes)(DOI)
42.
A. Bax, B.L. Hawkins and G.E. Maciel: Off-resonance cross-polarization: A technique to reduce rf power requirements for magnetization transfer experiments in solids. J. Magn. Reson. 59, 530-535 (1984). (42.pdf, 341974 Bytes)(DOI)
43.
A. Bax and S.K. Sarkar: Elimination of refocusing pulses in NMR experiments. J. Magn. Reson. 60, 170-176 (1984). (43.pdf, 398959 Bytes)(DOI)
44.
A.F. Mehlkopf, A. Bax, J. Smidt and T.A. Tiggelman: Design, control system and software organization of multipurpose NMR spectrometer control, data acquisition and on-line data processing. Computer Enhanced Spectroscopy 2, 133-144 (1984).
45.
A. Bax, R.A. Byrd and A. Aszalos: Spin multiplet enhancement in two-dimensional correlated NMR spectroscopy. J. Am. Chem. Soc. 106, 7632-7633 (1984). (45.pdf, 283004 Bytes)(DOI)
46.
A. Bax, W. Egan and P. Kovacs: New NMR techniques for structure determination and resonance assignments of complex carbohydrates. J. Carbohydr. Chem. 3, 593-611 (1984). (46.pdf, scanned, 656636 Bytes)(DOI)
47.
B. Borah, J.S. Cohen and A. Bax: Conformation of double stranded polydeoxynucleotides in solution by proton two-dimensional nuclear Overhauser enhancement spectroscopy. Biopolymers 24, 747-765 (1985). (47.pdf, 809142 Bytes)(DOI)(pubmed)
48.
A. Bax and G. Drobny: Optimization of two-dimensional homonuclear relayed coherence transfer NMR spectroscopy. J. Magn. Reson. 61, 306-320 (1985). (48.pdf, 858063 Bytes)(DOI)
49.
N.M. Szeverenyi, A. Bax and G.E. Maciel: Magic-angle hopping as an alternative to magic-angle spinning for solid state NMR. J. Magn. Reson. 61, 440-447 (1985). (49.pdf, 560233 Bytes)(DOI)
50.
S.K. Sarkar and A. Bax: A simple and sensitive one-dimensional NMR technique for correlation of proton and carbon chemical shifts. J. Magn. Reson. 62, 109-112 (1985). (50.pdf, 262642 Bytes)(DOI)
51.
A. Bax, J.A. Ferretti, N. Nashed and D.M. Jerina: Complete 1H and 13C NMR assignment of complex polycyclic aromatic hydrocarbons. J.Org. Chem. 50, 3029-3034 (1985). (51.pdf, 679104 Bytes)(DOI)
52.
A. Bax and D.G. Davis: Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63, 207-213 (1985). (52.pdf, 455261 Bytes)(DOI)
53.
A. Bax: A simple description of two-dimensional NMR spectroscopy. Bull. Magn. Reson. 7, 167-183 (1985). (53.pdf, 19038750 Bytes)
54.
D.G. Davis and A. Bax: Assignment of complex 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820-2821 (1985). (54.pdf, 262226 Bytes)(DOI)
55.
A. Bax, D.G. Davis and S.K. Sarkar: An improved method for two-dimensional heteronuclear relayed coherence transfer NMR spectroscopy. J. Magn. Reson. 63, 230-234 (1985). (55.pdf, 310015 Bytes)(DOI)
56.
S.K. Sarkar and A. Bax: Optimization of heteronuclear relayed coherence transfer spectroscopy. J. Magn. Reson. 63, 512-523 (1985). (56.pdf, 761968 Bytes)(DOI)
57.
D.G. Davis and A. Bax: Simplification of 1H NMR spectra by selective excitation of experimental subspectra. J. Am. Chem. Soc. 107, 7197-7l98 (1985). (57.pdf, 278553 Bytes)(DOI)
58.
R.H. Griffey, D. Davis, Z. Yamaizumi, S. Nishimura, A. Bax, B.L. Hawkins and C.D. Poulter: 15N-labeled Escherichia coli tRNAfMet, tRNAGlu, tRNATyr, and tRNAPhe: Double resonance and two-dimensional NMR of N1-labeled pseudouridine. J. Biol. Chem. 260, 9734-9741 (1985). (58.pdf, 926172 Bytes)(pubmed)
59.
A. Aszalos, A. Bax, N. Burlinson, P. Roller and C. McNeal: Physico-chemical and microbiological comparison of nystatin, amphotericin A and amphotericin B, and structure of amphotericin A. J. Antibiotics 38, 1699-1713 (1985). (59.pdf, 5524988 Bytes)(DOI)(pubmed)
60.
D.G. Davis and A. Bax: Separation of chemical exchange and cross-relaxation effects in two-dimensional NMR spectroscopy. J. Magn. Reson. 64, 533-535 (1985). (60.pdf, 173722 Bytes)(DOI)
61.
A. Bax: A spatially selective composite 90˚ radiofrequency pulse. J. Magn. Reson. 65, 142-145 (1985). (61.pdf, 210698 Bytes)(DOI)
62.
A. Bax and D.G. Davis: MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360 (1985). (62.pdf, 377054 Bytes)(DOI)
63.
N. Guirguis, R. Schneerson, A. Bax, W. Egan, J.B. Robbins, J. Shiloach, I. Orskov, F. Orskov, and A. El Kholy: Escherichia coli K51 and K93 capsular polysaccharides are cross-reactive with the group A capsular polysaccharide of Neisseria meningitidis. Immunochemical, biological and epidemiological studies. J. Exp. Med. 162, 1837-1851 (1985).(63.pdf, 2294139 Bytes)(pubmed)
64.
A. Bax: Two-dimensional NMR spectroscopy. In "NMR in Living Systems," T. Axenrod and G. Ceccarelli, (Eds.), Reidel, Dordrecht, 1986, pp. 67-94.
M.W. Edwards and A. Bax: Complete Proton and carbon-13 NMR assignment of the alkaloid gephyrotoxin through the use of homonuclear Hartmann-Hahn and two-dimensional spectroscopy. J. Am. Chem. Soc. 108, 918-923 (1986). (66.pdf, 788190 Bytes)(DOI)
67.
S. Ito, H. Ziffer and A. Bax: On the relation between ring size and geometry of 2-bromo-2-cycloalkenyl acetates formed from dibromobicyclo[n.1.0]alkanes by silver acetate catalyzed reactions. Use of 3J(C-H) couplings to assign the geometry of trisubstituted olefins. J. Org. Chem. 51, 1130-1133 (1986). (67.pdf, 532749 Bytes)(DOI)
68.
A. Bax and D.G. Davis: Homonuclear Hartmann-Hahn magnetization transfer: New one-and two-dimensional NMR methods for structure determination and spectral assignment. In "Advanced Magnetic Resonance Techniques in Systems of High Molecular Complexity," N. Niccolai and G. Valensin, (Eds.), Birkhauser, Basel, 1986, pp. 21-48. (68.pdf, scanned, 515751 Bytes)
69.
A. Bax and M.F. Summers: 1H and 13C assignments from sensitivity enhanced detection of heteronuclear multiple-bond connectivity by two-dimensional multiple quantum NMR. J. Am. Chem. Soc. 108, 2093-2094 (1986). (69.pdf, 294296 Bytes)(DOI)
70.
T.H. Mareci, W. Sattin, K.N. Scott and A. Bax: Tip angle reduced T1 imaging. J. Magn. Reson. 67, 55-65 (1986). (70.pdf, 2395747 Bytes)(DOI)
71.
A. Bax and S. Subramanian: Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy. J. Magn. Reson. 67, 565-570 (1986). (71.pdf, 331073 Bytes)(DOI)
72.
M.F. Summers, L.G. Marzilli and A. Bax: Complete 1H and 13C assignment of coenzyme B12 through the use of new two-dimensional NMR experiments. J. Am. Chem. Soc. 108, 4285-4294 (1986). (72.pdf, 1294192 Bytes)(DOI)
73.
L. Lerner and A. Bax: Sensitivity-enhanced two-dimensional heteronuclear relayed coherence transfer NMR spectroscopy. J. Magn. Reson. 69, 375-380 (1986). (73.pdf, 450857 Bytes)(DOI)
74.
A. Bax, A. Aszalos, Z. Dinya and K. Sudo: Structure elucidation of the antibiotic Four-d mycin through the use of new two-dimensional NMR techniques. J. Am. Chem. Soc. 108, 8056-8063 (1986). (74.pdf, 984966 Bytes)(DOI)
75.
A. Bax, V. Sklenar and M.F. Summers: Direct identification of relayed nuclear Overhauser effects. J. Magn. Reson. 70, 327-331 (1986). (75.pdf, 318304 Bytes)(DOI)
76.
V. Sklenar, H. Miyashiro, G. Zon, H.T. Miles and A. Bax: Assignment of the 31P and 1H resonances in oligonucleotides by two-dimensional NMR spectroscopy. FEBS Lett. 208, 94-98 (1986). (76.pdf, 358505 Bytes)(DOI)(pubmed)
77.
E. Falent-Kwast, P. Kovacs, A. Bax and P.J. Glaudemans: Synthesis of b,c-epoxypropyl 0-(b-D-galactopyranosyl)-(1\6)- b-D-galactopyranoside. Carbohydr. Res. 145, 332-340 (1986). (77.pdf, 581369 Bytes)(DOI)(pubmed)
78.
S.K. Sarkar, J.D. Glickson and A. Bax: Assignment of secondary amide 15N resonances of bleomycin-A2 by two-dimensional multiple quantum 1H-15H shift correlation NMR spectroscopy. J. Am. Chem. Soc. 108, 6814-6816 (1986). (78.pdf, 408857 Bytes)(DOI)
79.
L. Lerner and A. Bax: Application of new, high-sensitivity 1H-13C-NMR spectral techniques to the study of oligosaccharides. Carbohydr. Res. 166, 35-46 (1987). (79.pdf, 743988 Bytes)(DOI)(pubmed)
80.
S. Subramanian and A. Bax: Generation of pure phase NMR subspectra for measurement of homonuclear coupling constants. J. Magn. Reson. 71, 325-330 (1987). (80.pdf, 426088 Bytes)(DOI)
81.
R. A. Byrd, W. Egan, M.F. Summers and A. Bax: New NMR spectroscopic approaches for structural studies of polysaccharides: Application to the haemophilus influenza type A capsular poly-saccharide. Carbohydr. Res. 166, 47-58 (1987). (81.pdf, 819658 Bytes)(DOI)(pubmed)
82.
V. Sklenar and A. Bax: Two-dimensional heteronuclear chemical-shift correlation of proteins at natural abundance 15N and 13C levels. J. Magn. Reson. 71, 379-383 (1987). (82.pdf, 565058 Bytes)(DOI)
83.
A. Bax and M. Weiss: Simplification of two-dimensional NOE spectra of proteins by 13C labeling. J. Magn. Reson. 71, 571-575 (1987). (83.pdf, 307482 Bytes)(DOI)
84.
A. Bax, L.G. Marzilli and M.F. Summers: New insights into the solution behavior of cobalamins: Studies of the base-off form of coenzyme B12 using modern two-dimensional NMR methods. J. Am. Chem. Soc. 109, 566-574 (1987). (84.pdf, 1122853 Bytes)(DOI)
85.
V. Sklenar, A. Bax and G. Zon: Assignment of Z DNA NMR spectra of poly d(Gm5dC) and 2D multinuclear NMR spectroscopy. J. Am. Chem. Soc. 109, 2221-2222 (1987). (85.pdf, 283186 Bytes)(DOI)
86.
V. Sklenar, D.A. Torchia and A. Bax: Measurement of carbon-13 longitudinal relaxation using 1H detection. J. Magn. Reson. 73, 375-379 (1987). (86.pdf, 368966 Bytes)(DOI)
87.
V. Sklenar and A. Bax: Spin echo water suppression for the generation of pure phase two-dimensional NMR spectra. J. Magn. Reson. 74, 469-479 (1987). (87.pdf, 713824 Bytes)(DOI)
88.
V. Sklenar, R. and A. Bax: Water suppression using a combination of hard and soft pulses. J. Magn. Reson. 75, 352-357 (1987). (88.pdf, 374862 Bytes)(DOI)
89.
V. Sklenar, B.R. Brooks, G. Zon and A. Bax: Absorption mode two-dimensional NOE spectroscopy of exchangeable protons in oligonucleotides. FEBS Lett. 216, 249-252 (1987). (89.pdf, 353731 Bytes)(DOI)(pubmed)
90.
A. Bax, V. Sklenar, A.M. Gronenborn and G.M. Clore: Water suppression in two-dimensional spin-locked NMR experiments using a novel phase cycling procedure. J. Am. Chem. Soc. 109, 6511-6513 (1987). (90.pdf, 448654 Bytes)(DOI)
91.
V. Sklenar and A. Bax: A new water suppression technique for generating pure phase spectra with equal excitation over a wide bandwidth. J. Magn. Reson. 75, 378-383 (1987). (91.pdf, 335227 Bytes)(DOI)
92.
V. Sklenar and A. Bax: Measurement of 1H-31P NMR coupling constants in double-stranded DNA fragments. J. Am. Chem. Soc. 109, 7525-7526 (1987). (92.pdf, 277322 Bytes)(DOI)
93.
A. Bax, M.F. Summers, W. Egan, N. Guirgis, R. Schneerson, J.B. Robbins, F. Orskov, I. Orskov and W.F. Vann: Structural studies of the Escherichia coli K93 and K53 capsular poly-saccharides. Carbohydr. Res. 173, 53-64 (1988). (93.pdf, 880263 Bytes)(DOI)(pubmed)
94.
D. Williamson and A. Bax: Resolution enhanced correlation of 1H and 31P chemical shifts. J. Magn. Reson. 76, 174-177 (1988). (94.pdf, 309661 Bytes)(DOI)
95.
A. Bax: Correction of cross peak intensities in 2D spin-locked NOE spectroscopy for offset and Hartmann-Hahn effects. J. Magn. Reson. 77, 134-147 (1988). (95.pdf, 967526 Bytes)(DOI)
96.
H. Ziffer, A. Bax, R.J. Highet and B. Green: Investigation by two-dimensional NMR of the structure and stereochemistry of a methyl p-nitrocinnamate photodimer. J. Org. Chem. 53, 895-896 (1988). (96.pdf, 278190 Bytes)(DOI)
97.
D. Marion, M. Zasloff and A. Bax: A two-dimensional NMR study of the antimicrobial peptide Magainin 2. FEBS Lett. 227, 21-26 (1988). (97.pdf, 391182 Bytes)(DOI)(pubmed)
98.
A. Bax and D. Marion: Improved resolution and sensitivity in 1H-detected heteronuclear multiple-bond correlation spectroscopy. J. Magn. Reson. 78, 186-191 (1988). (98.pdf, 400440 Bytes)(DOI)
99.
D.A. Torchia, S.W. Sparks and A. Bax: Delineation of alpha-helical domains in deuteriated staphylococcal nuclease by 2D NOE NMR spectroscopy. J. Am. Chem. Soc. 110, 2320-2321 (1988). (99.pdf, 308378 Bytes)(DOI)
100.
D. Marion and A. Bax: Baseline distortion in real-Fourier-transform NMR spectra. J. Magn. Reson. 79, 352-356 (1988). (100.pdf, 276977 Bytes)(DOI)
101.
A. Bax and L. Lerner: Measurement of 1H-1H coupling constants in DNA fragments by 2D NMR. J. Magn. Reson. 79, 429-438 (1988). (101.pdf, 607075 Bytes)(DOI)
102.
D.A. Torchia, S.W. Sparks and A. Bax: NMR signal assignments of amide protons in the alpha-helical domains of staphylococcal nuclease. Biochemistry 27, 5135-5141 (1988). (102.pdf, 798892 Bytes)(DOI)(pubmed)
103.
G.M. Clore, A. Bax, P. Wingfield and A M. Gronenborn: Long-range 15N-1H correlation as an aid to sequential proton resonance assignment of proteins: Application to the DNA-binding protein ner from phage Mu. FEBS Lett. 238, 17-21 (1988). (103.pdf, 474728 Bytes)(DOI)(pubmed)
104.
A. Bax, S.W. Sparks and D.A. Torchia: Long-range heteronuclear correlation: A powerful tool for the NMR analysis of medium-size proteins. J. Am. Chem. Soc. 110, 7926-7929 (1988). (104.pdf, 292088 Bytes)(DOI)
105.
D. Marion and A. Bax: P.COSY: A sensitive alternative for double-quantum filtered COSY. J. Magn. Reson. 80, 528-533 (1988). (105.pdf, 374061 Bytes)(DOI)
106.
F. Inagaki, I. Shimada, D. Kohda, A. Suzuki and A. Bax: Relayed HOHAHA: A useful method for extracting subspectra of individual components of sugar chains. J. Magn. Reson. 81, 186-190 (1989). (106.pdf, 280468 Bytes)(DOI)
A. Bax: Homonuclear magnetization transfer experiments using isotropic and non-isotropic mixing schemes. Isr. J. Chem. 28, 309-317 (1989). (109.pdf, scanned, 274138 Bytes)
A. Bax, L.E. Kay, S.W. Sparks and D.A. Torchia.: Line narrowing of amide proton resonances in 2D NMR spectra of proteins. J. Am. Chem. Soc. 111, 408-409 (1989). (111.pdf, 242537 Bytes)(DOI)
112.
D. Marion, L.E. Kay, S.W. Sparks, D.A. Torchia and A. Bax: Three-dimensional heteronuclear NMR of 15N labeled proteins. J. Am. Chem. Soc. 111, 1515-1517 (1989). (112.pdf, 373962 Bytes)(DOI)
113.
A.M. Gronenborn, A. Bax, P.T. Wingfield and G.M. Clore: A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy. FEBS Lett. 243, 93-98 (1989). (113.pdf, 312094 Bytes)(DOI)(pubmed)
114.
D. Marion and A. Bax: Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time domain data. J. Magn. Reson. 83, 205-211 (1989). (114.pdf, 485782 Bytes)(DOI)
115.
L.E. Kay, D. Marion and A. Bax: Practical aspects of three-dimensional heteronuclear NMR of proteins. J. Magn. Reson. 84, 72-84 (1989). (115.pdf, 976762 Bytes)(DOI)
115b.
D. Marion, M. Ikura and A. Bax: Improved solvent suppression in one- and two-dimensional NMR spectra by convolution of time domain data. J. Magn. Reson. 84, 425-430 (1989). (115b.pdf, 445623 Bytes)(DOI)
116.
L.E. Kay and A. Bax: Separation of NH and NH2 resonances in 1H detected heteronuclear multiple quantum correlation spectra. J. Magn. Reson. 84, 598-603 (1990). (116.pdf, 348241 Bytes)(DOI)
117.
D.A. Torchia, S.W. Sparks and A. Bax: Staphylococcal nuclease: Sequential assignments and solution structure. Biochemistry 28, 5509-5524 (1989).(117.pdf, 1706088 Bytes)(DOI)(pubmed)
118.
L.E. Kay and A. Bax: New methods for the measurement of NH-CaH J couplings in 15N labeled proteins. J. Magn. Reson. 86, 110-126 (1990). (118.pdf, 1064564 Bytes)(DOI)
119.
L.E. Kay, B. Brooks, S.W. Sparks, D.A. Torchia and A. Bax: Measurement of NH-CaH coupling constants in staphylococcal nuclease by two-dimensional NMR and comparison with X-ray crystallographic results. J. Am. Chem. Soc. 111, 5488-5490 (1989). (119.pdf, 379524 Bytes)(DOI)
120.
D. Williamson, I.J. McLennan, A. Bax, M.P. Gamcsik and J.D. Glickson: Two-dimensional NMR study of Bleomycin and its zinc(II) complex: Reassignment of carbon-13 resonances. J. Biomolec. Struct. Dyn. 8, 375-398 (1990). (120.pdf, scanned, 373978 Bytes)(DOI)(pubmed)
121.
A. Bax, M. Ikura, L.E. Kay, D.A. Torchia and R. Tschudin: Comparison of different modes of two-dimensional reverse correlation NMR for the study of proteins. J. Magn. Reson. 86, 304-318 (1990). (121.pdf, 1036072 Bytes)(DOI)
122.
D. Marion, P.C. Driscoll, L.E. Kay, P.T. Wingfield, A. Bax, A.M. Gronenborn and G.M. Clore: Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins using three-dimensional homonuclear Hartmann-Hahn and nuclear Overhauser-1H-15N heteronuclear multiple quantum coherence spectroscopy. Biochemistry 28, 6150-6156 (1989). (122.pdf, 856956 Bytes)(DOI)(pubmed)
123.
L.E. Kay, D.A. Torchia and A. Bax: Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease. Biochemistry 28, 8972-8979 (1989). (123.pdf, 1002509 Bytes)(DOI)(pubmed)
124.
D.A. Torchia, S.W. Sparks, P.E. Young and A. Bax: Proline Assignments and identification of the Cis K116/P117 peptide bond in liganded staphylococcal nuclease using isotope edited 2D NMR spectroscopy. J. Am. Chem. Soc. 111, 8315-8317 (1989). (124.pdf, 970192 Bytes)(DOI)
125.
M. Ikura, L.E. Kay and A. Bax: Three-dimensional NOESY-HMQC spectroscopy of a 13C-labeled protein. J. Magn. Reson. 86, 204-209 (1990). (125.pdf, 415233 Bytes)(DOI)
126.
L.E. Kay, M. Ikura and A. Bax: Proton-proton correlation via carbon-carbon coupling: A three-dimensional NMR approach for the assignment of aliphatic resonances in proteins labeled with carbon-13. J. Am. Chem. Soc. 112, 888-889 (1990). (126.pdf, 309109 Bytes)(DOI)
M. Ikura, D. Marion, L.E. Kay, H. Shih, M. Krinks, C.B. Klee and A. Bax: Heteronuclear 3D NMR and isotopic labeling of calmodulin: Towards the complete assignment of the 1H NMR spectrum. J. Biochem. Pharm. 40, 153-160 (1990). (128.pdf, 953732 Bytes)(DOI)(pubmed)
129.
D. Marion, M. Ikura, R. Tschudin and A. Bax: Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85, 393-399 (1989). (129.pdf, 522778 Bytes)(DOI)
130.
M. Ikura, M. Krinks, D.A. Torchia and A. Bax: An efficient NMR approach for obtaining sequence-specific resonance assignments in larger proteins based on multiple isotopic labeling. FEBS Lett. 266, 155-158 (1990). (130.pdf, 322707 Bytes)(DOI)(pubmed)
131.
A. Bax, M. Ikura, L.E. Kay and G. Zhu: Removal of F1 Baseline distortion and optimization of folding in multi-dimensional NMR spectroscopy. J. Magn. Reson. 91, 174-178 (1991). (131.pdf, 319433 Bytes)(DOI)
132.
G. Zhu and A. Bax: Improved linear prediction for truncated signals of known phase. J. Magn. Reson. 90, 405-410 (1990). (132.pdf, 416921 Bytes)(DOI)
133.
A. Bax, G.M. Clore, P.C. Driscoll, A.M. Gronenborn, M. Ikura and L.E. Kay: Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins. J. Magn. Reson. 87, 620-627 (1990). (133.pdf, 595637 Bytes)(DOI)
134.
L.E. Kay, G.M. Clore, A. Bax and A.M. Gronenborn: Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1b in solution. Science 249, 411-414 (1990). (134.pdf, 998482 Bytes)(DOI)(pubmed)
135.
M. Ikura, L.E. Kay and A. Bax: A novel approach for sequential assignment of 1H, 13C, and 15N spectra of larger proteins: Heteronuclear triple-resonance NMR spectroscopy. application to calmodulin. Biochemistry 29, 4659-4667 (1990). (135.pdf, 1855442 Bytes)(DOI)(pubmed)
136.
G.M. Clore, A. Szabo, A. Bax, L.E. Kay, P.C. Driscoll and A.M. Gronenborn: Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 muclear magnetic relaxation of proteins. J. Am. Chem. Soc. 112, 4989-4991 (1990). (136.pdf, 366235 Bytes)(DOI)
137.
A. Bax, G.M. Clore and A.M. Gronenborn: 1H-1H correlation via isotropic mixing of 13C magnetization: A new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins. J. Magn. Reson. 88, 425-431 (1990). (137.pdf, 519592 Bytes)(DOI)
138.
G.M. Clore, A. Bax, P.C. Driscoll, P.T. Wingfield and A.M. Gronenborn: Assignment of the side chain 1H and 13C resonances of interleukin-1b using double and triple resonance heteronuclear three-dimensional NMR spectroscopy. Biochemistry 29, 8172-8184 (1990). (138.pdf, 1766520 Bytes)(DOI)(pubmed)
139.
L.E. Kay, M. Ikura, R. Tschudin and A. Bax: Three-dimensional triple resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89, 496-514 (1990). (139.pdf, 1422787 Bytes)(DOI)
140.
G.M. Clore, A. Bax, P.T. Wingfield and A.M. Gronenborn: Identification and localization of bound internal water in the solution structure of interleukin-1b by heteronuclear three-dimensional rotating frame Overhauser 15N-1H multiple quantum coherence NMR spectroscopy. Biochemistry 29, 5671-5676 (1990). (140.pdf, 757604 Bytes)(DOI)(pubmed)
141.
M. Ikura, A. Bax, G.M. Clore and A.M. Gronenborn: Detection of nuclear Overhauser effects between degenerate amide protons by heteronuclear three-dimensional NMR spectroscopy. J. Am. Chem. Soc. 112, 9020-9022 (1990). (141.pdf, 432224 Bytes)(DOI)
142.
Y. Osawa, R.J. Highet, A. Bax and L.R. Pohl: Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. J. Biol. Chem. 266, 3208-3214 (1991). (142.pdf, 2150967 Bytes)(pubmed)
143.
C.P.J. Glaudemans, L. Lerner, G.D. Daves, P. Kovac, R. Venable and A. Bax: Significant conformational changes in an antigenic carbohydrate epitope upon binding to a monoclonal antibody. Biochemistry 29, 10906-10911 (1990). (143.pdf, 824837 Bytes)(DOI)(pubmed)
144.
G.M. Clore, L.E. Kay, A. Bax and A.M. Gronenborn: Four-dimensional 13C/13C-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: Application to interleukin-1b. Biochemistry 30, 12-18 (1991). (144.pdf, 840282 Bytes)(DOI)(pubmed)
145.
L.E. Kay, M. Ikura and A. Bax: The design and optimization of complex NMR experiments: Application to a triple resonance pulse scheme correlating Ha, NH and 15N chemical shifts in 15N-13C labeled proteins. J. Magn. Reson. 91, 84-92 (1991). (145.pdf, 626891 Bytes)(DOI)
146.
L.E. Kay, M. Ikura, G. Zhu and A. Bax: Four-dimensional heteronuclear triple resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms. J. Magn. Reson. 91, 422-428 (1991). (146.pdf, 501679 Bytes)(DOI)
147.
S. Spera, M. Ikura and A. Bax: Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment. J. Biomol. NMR 1, 155-165 (1991). (147.pdf, 694740 Bytes)(DOI)(pubmed)
148.
A. Bax and M. Ikura: An efficient three-dimensional NMR technique for correlating the proton and nitrogen backbone amide resonances with the alpha carbon of the preceeding residue in uniformly 13C/15N enriched proteins. J. Biomol. NMR 1, 99-104 (1991). (148.pdf, 497674 Bytes)(DOI)(pubmed)
149.
S. Spera and A. Bax: An empirical correlation between protein backbone conformation and Ca and Cb chemical shifts. J. Am. Chem. Soc. 113, 5490-5492 (1991). (149.pdf, 419913 Bytes)(DOI)
150.
M. Ikura, L.E. Kay, M. Krinks and A. Bax: A triple resonance NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light chain kinase: Indication of a conformational change in the central helix. Biochemistry 30, 5498-5504 (1991). (150.pdf, 1463938 Bytes)(DOI)(pubmed)
151.
G.M. Clore, A. Bax and A.M. Gronenborn: Stereospecific assignment of Cb-methylene protons in larger proteins using three-dimensional 15N separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy. J. Biomol. NMR 1, 13-22 (1991). (151.pdf, 631951 Bytes)(DOI)(pubmed)
152.
R. Powers, G.M. Clore, A. Bax, D.S. Garrett, S.J. Stahl, P.T. Wingfield and A.M. Gronenborn: Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. J. Mol. Biol. 221, 1081-1090 (1991). (152.pdf, 1621359 Bytes)(DOI)(pubmed)
153.
R. Powers, A.M. Gronenborn, G.M. Clore and A. Bax: Three-dimensional triple resonance NMR of 13C/15N enriched proteins using constant-time evolution. J. Magn. Reson. 94, 209-213 (1991). (153.pdf, 357331 Bytes)(DOI)
154.
M. Ikura, S. Spera, G. Barbato, L.E. Kay, M. Krinks and A. Bax: Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multi-dimensional NMR spectroscopy. Biochemistry 30, 9216-9228 (1991). (154.pdf, 1988407 Bytes)(DOI)(pubmed)
155.
M. Ikura, L.E. Kay and A. Bax: Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C labeled protein using constant-time evolution. J. Biomol. NMR 1, 299-304 (1991). (155.pdf, 379137 Bytes)(DOI)(pubmed)
156.
F. Delaglio, D.A. Torchia and A. Bax: Measurement of nitrogen-15 carbon-13 J couplings in Staphylococcal nuclease. J. Biomol. NMR 1, 439-446 (1991). (156.pdf, 397883 Bytes)(DOI)(pubmed)
157.
A. Bax, M. Ikura, L.E. Kay, G. Barbato and S. Spera: Multi-dimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: A powerful new strategy for structure determination. In "Protein Conformation," Wiley, Chichester (Ciba Foundation Symposium 161), 1991, pp.108-119. (157.pdf, scanned, 185893 Bytes)
158.
M. Ikura and A. Bax: Isotope filtered 2D NMR of a protein-peptide complex: Study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin. J. Am. Chem. Soc. 114, 2433-2440 (1992). (158.pdf, 825764 Bytes)(DOI)
159.
S.J. Archer, M. Ikura, D.A. Torchia and A. Bax: An alternative 3D NMR technique for correlating backbone 15N with side chain Hb resonances in larger proteins. J. Magn. Reson. 95, 636-641 (1991). (159.pdf, 358748 Bytes)(DOI)
160.
A. Bax: Experimental NMR techniques for studies of biopolymers. Cur. Opinion Struct. Biol. 1, 1030-1035 (1991). (160.pdf, 640841 Bytes)(DOI)
161.
S. Grzesiek, M. Ikura, G.M. Clore, A.M. Gronenborn and A. Bax: A 3D triple resonance NMR technique for qualitative measurement of carbonyl-Hb J couplings in isotopically enriched proteins. J. Magn. Reson. 96, 215-221 (1992). (161.pdf, 652902 Bytes)(DOI)
162.
S. Grzesiek and A. Bax: Improved 3D triple resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96, 432-440 (1992). (162.pdf, 596221 Bytes)(DOI)
163.
L.E. Kay, L.K. Nicholson, F. Delaglio, A. Bax and D.A. Torchia: Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins. J. Magn. Reson. 97, 359-375 (1992). (163.pdf, 1174164 Bytes)(DOI)
164.
G. Barbato, M. Ikura, L.E. Kay, R. W. Pastor and A. Bax: Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31, 5269-5278 (1992). (164.pdf, 1843959 Bytes)(164_SI.pdf, 204538 Bytes)(DOI)(pubmed)
165.
L. Nicholson, L.E. Kay, D.M. Baldisseri, J. Arango, P.E. Young, A. Bax and D.A. Torchia: Dynamics of methyl groups in proteins as studied by 13C NMR spectroscopy. Application to the leucine residues of Staphylococcal nuclease. Biochemistry 31, 5253-5263 (1992). (165.pdf, 1966835 Bytes)(DOI)(pubmed)
166.
G.W. Vuister and A. Bax: Resolution enhancement and spectral editing of uniformly 13C enriched proteins by homonuclear broadband 13C-13C decoupling. J. Magn. Reson. 98, 428-435 (1992). (166.pdf, 620151 Bytes)(DOI)
167.
M. Ikura, G.M. Clore, A.M. Gronenborn, G. Zhu, C.B. Klee and A. Bax: Solution structure of a calmodulin-target peptide complex by multi-dimensional NMR. Science 256, 632-638 (1992). (167.pdf, 2207546 Bytes)(DOI)(pubmed)
168.
G. Zhu and A. Bax: Two-dimensional linear prediction for signals truncated in both dimensions. J. Magn. Reson. 98, 192-199 (1992). (168.pdf, 594160 Bytes)(DOI)
169.
A. Bax, D. Max and D. Zax: Measurement of multiple-bond 13C-13C J couplings in a 20-kDa protein-peptide complex. J. Am. Chem. Soc. 114, 6923-6925 (1992). (169.pdf, 406489 Bytes)(DOI)
170.
G.W. Vuister, F. Delaglio and A. Bax: An empirical correlation between 1JCaHa and protein backbone conformation. J. Am. Chem. Soc. 114, 9674-9675 (1992). (170.pdf, 247177 Bytes)(DOI)
171.
S. Grzesiek and A. Bax: Correlating backbone amide and sidechain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114, 6291-6293 (1992). (171.pdf, 388834 Bytes)(DOI)
172.
M. Ikura, G. Barbato, C.B. Klee and A. Bax: Solution structure of calmodulin and its complex with a myosin light chain kinase fragment. Cell Calcium 13, 391-400 (1992). (172.pdf, 2793139 Bytes)(DOI)(pubmed)
173.
S. Grzesiek, H. Doebeli, R. Gentz, G. Garotta, A.M. Labhardt, and A. Bax: 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-g. Biochemistry 31, 8180-8190 (1992). (173.pdf, 1253310 Bytes)(DOI)(pubmed)
174.
G.W. Vuister and A. Bax: Measurement of two-bond JCOHa coupling constants in proteins uniformly enriched with 13C. J. Biomol. NMR 2, 401-405 (1992). (174.pdf, 324472 Bytes)(DOI)(pubmed)
175.
S. Grzesiek and A. Bax: An efficient experiment for sequential backbone assignment of medium sized isotopically enriched proteins. J. Magn. Reson. 99, 201-207 (1992). (175.pdf, 477737 Bytes)(DOI)
176.
A. Bax and S. Pochapsky: Optimized recording of heteronuclear multi-dimensional NMR spectra using pulsed field gradients. J. Magn. Reson. 99, 638-643 (1992). (176.pdf, 432094 Bytes)(DOI)
177.
P.R. Blake, M.F. Summers, M.W.W. Adams, J.-B. Park, Z.H. Zhou and A. Bax: Quantitative measurement of small through-hydrogen-bond and "through-space" J couplings in metal-substituted rubredoxin from Pyrococcus furiosus. J. Biomol. NMR 2, 527-533 (1992). (177.pdf, 392881 Bytes)(DOI)(pubmed)
178.
G. Zhu and A. Bax: Improved linear prediction of damped NMR signals using modified "forward-backward" linear prediction. J. Magn. Reson. 100, 202-207 (1992). (178.pdf, 329939 Bytes)(DOI)
179.
G.W. Vuister, F. Delaglio and A. Bax: The use of 1JCaHa coupling constants as a probe for protein backbone conformation. J. Biomol. NMR 3, 67-80 (1993). (179.pdf, 858428 Bytes)(DOI)(pubmed)
180.
L.E. Kay, T.E. Bull, L.K. Nicholson, C. Griesinger, H. Schwalbe, A. Bax and D.A. Torchia: The measurement of heteronuclear transverse relaxation times in AX3 systems via polarization transfer techniques. J. Magn. Reson. 100, 538-558 (1992). (180.pdf, 1530934 Bytes)(DOI)
181.
A. Bax and S. Grzesiek: Methodological advances in protein NMR. Acc. Chem. Res. 26, 131-138 (1993). (181.pdf, 1047680 Bytes)(DOI)
182.
S. Grzesiek and A. Bax: Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N enriched proteins. J. Biomol. NMR 3, 185-204 (1993). (182.pdf, 1219330 Bytes)(DOI)(pubmed)
183.
J. Anglister, S. Grzesiek, H. Ren, C.B. Klee and A. Bax: Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS.J. Biomol. NMR 3, 121-126 (1993). (183.pdf, 390674 Bytes)(DOI)(pubmed)
184.
S. Grzesiek, J. Anglister and A. Bax: Correlation of backbone amide and aliphatic sidechain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J. Magn. Reson. B 101, 114-119 (1993). (184.pdf, 398694 Bytes)(DOI)
185.
G.W. Vuister, G.M. Clore, A.M. Gronenborn, R. Powers, D.S. Garrett, R. Tschudin and A. Bax: Increased resolution and improved spectral quality in four-dimensional 13C/13C separated HMQC-NOESY-HMQC spectra using pulsed field gradients. J. Magn. Reson. B 101, 210-213 (1993). (185.pdf, 365829 Bytes)(DOI)
186.
N.T. Nashed, A. Bax, R.J. Loncharich, J.M. Sayer and D.M. Jerina: Methanolysis of K-region arene oxides: Comparison between acid-catalyzed and methoxide ion addition reactions. J. Am. Chem. Soc. 115, 1711-1722 (1993). (186.pdf, 1908417 Bytes)(DOI)
187.
A. Bax, G.W. Vuister, S. Grzesiek, F. Delaglio, A.C. Wang, R. Tschudin and G. Zhu: Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Meth. Enzymol. 239, 79-105 (1994). (187.pdf, 1373583 Bytes)(DOI)(pubmed)
188.
S. Grzesiek, J. Anglister, H. Ren and A. Bax: 13C line narrowing by 2H decoupling in 2H/13C/15N enriched proteins. Application to triple resonance 4D J connectivity of sequential amides.J. Am. Chem. Soc. 115, 4369-4370 (1993). (188.pdf, 268695 Bytes)(DOI)
189.
G.W. Vuister, A.C. Wang and A. Bax: Measurement of three-bond nitrogen-carbon J couplings in proteins uniformly enriched in 15N and 13C. J. Am. Chem. Soc. 115, 5334-5335 (1993). (189.pdf, 242953 Bytes)(DOI)
190.
G.W. Vuister and A. Bax: Quantitative J correlation: A new approach for measuring homonuclear three bond J(HNHa) coupling constants in 15N-enriched proteins.J. Am. Chem. Soc. 115, 7772-7777 (1993). (190.pdf, 701161 Bytes)(DOI)
191.
S. Grzesiek, G.W. Vuister and A. Bax: A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins. J. Biomol. NMR 3, 487-493 (1993). (191.pdf, 418838 Bytes)(DOI)(pubmed)
192.
G. Zhu, D.A. Torchia and A. Bax: Discrete Fourier transformation of NMR signals. The relationship between sampling delay and spectral baseline. J. Magn. Reson. A 105, 219-222 (1993). (192.pdf, 255700 Bytes)(DOI)
193a.
G.W. Vuister, T. Yamazaki, D.A. Torchia and A. Bax: Measurement of two- and three-bond 13C-1H J couplings to the Cd carbons of residues in Staphylococcal nuclease. J. Biomol. NMR 3, 297-306 (1993). (193.pdf, 676159 Bytes)(DOI)(pubmed)
193b.
S. Grzesiek and A. Bax: The origin and removal of artifacts in 3D HCACO spectra of proteins uniformly enriched with 13C. J. Magn. Reson. B 102, 103-106 (1993). (193b.pdf, 287697 Bytes)(DOI)
194.
G.W. Vuister and A. Bax: Measurement of two- and three-bond proton to methyl-carbon J couplings in proteins uniformly enriched with 13C. J. Magn. Reson. B 102, 228-231 (1993). (194.pdf, 319123 Bytes)(DOI)
195.
G.W. Vuister and A. Bax: Measurement of four-bond HN-Ha J couplings in Staphylococcal nuclease. J. Biomol. NMR 4, 193-200 (1994). (195.pdf, 524021 Bytes)(DOI)(pubmed)
196.
A.C. Wang and A. Bax: Minimizing the effects of radio-frequency heating in multi-dimensional NMR experiments. J. Biomol. NMR 3, 715-720 (1993). (196.pdf, 379204 Bytes)(DOI)(pubmed)
197.
J. Qin, F. Delaglio, G.N. La Mar and A. Bax: Distinguishing the effects of cross correlation and J coupling in COSY spectra of paramagnetic proteins. J. Magn. Reson. B 102, 332-336 (1993). (197.pdf, 380460 Bytes)(DOI)
198.
J. Anglister, S. Grzesiek, A.C. Wang, H. Ren, C.B. Klee and A. Bax: 1H, 13C, and 15N NMR backbone assignments and secondary structure of human calcineurin B. Biochemistry 33, 3540-3547 (1994). (198.pdf, 1096604 Bytes)(DOI)(pubmed)
199.
S. Grzesiek and A. Bax: Measurement of amide proton exchange rates and NOE with water in 13C/15N enriched calcineurin B. J. Biomol. NMR 3, 627-638 (1993). (199.pdf, 712209 Bytes)(DOI)(pubmed)
200.
S. Grzesiek and A. Bax: The importance of not saturating H2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115, 12593-12594 (1993). (200.pdf, 755602 Bytes)(DOI)
201.
S.J. Archer, A. Bax, A.B. Roberts, M.B. Sporn, Y. Ogawa, K.A. Piez, J.A. Weatherbee, M.L.-S. Tsang, R. Lucas, B.-L. Zheng, J. Wenker and D.A. Torchia: Transforming growth factor b1: NMR signal assignments of the recombinant protein expressed and isotopically enrcihed using Chinese hamster ovary cells. Biochemistry 32, 1152-1163 (1993). (201.pdf, 1253083 Bytes)(DOI)(pubmed)
202.
S.J. Archer, A. Bax, A.B. Roberts, M.B. Sporn, Y. Ogawa, K.A. Piez, J.A. Weatherbee, M.L.-S. Tsang, R. Lucas, B.-L. Zheng, J. Wenker and D.A. Torchia: Transforming growth factor b1: Secondary structure as determined by heteronuclear magnetic resonance spectroscopy. Biochemistry 32, 1164-1171 (1993). (202.pdf, 984618 Bytes)(DOI)(pubmed)
203.
G. Zhu and A. Bax: Measurement of long-range 1H-13C coupling constants from quantitative 2D heteronuclear multiple-quantum correlation spectra. J. Magn. Reson. A 104, 353-357 (1993). (203.pdf, 332241 Bytes)(DOI)
204.
S. Grzesiek, L.K. Nicholson, T. Yamazaki, P.Wingfield, S.J. Stahl, C.J. Eyermann, C.N. Hodge, P.Y.S. Lam, P.K. Jadhav, C.-H. Chang, D.A. Torchia and A. Bax: NMR evidence for the displacement of a conserved interior water molecule in HIV protease by a non-peptide cyclic urea based inhibitor. J. Am. Chem. Soc. 116, 1581-1582 (1994). (204.pdf, 281048 Bytes)(DOI)
205.
A. Bax, S. Grzesiek, A.M. Gronenborn and G.M. Clore: Isotope-filtered 2D HOHAHA spectroscopy of a peptide-protein complex using heteronuclear Hartmann-Hahn dephasing. J. Magn. Reson. A 106, 269-273 (1994). (205.pdf, 301864 Bytes)(DOI)
206.
G.W. Vuister, S.-J. Kim, C. Wu and A. Bax: NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF3/forkhead families of transcription factors. Biochemistry 33, 10-16 (1994). (206.pdf, 201405 Bytes)(DOI)(pubmed)
207.
G.M. Clore, A. Bax, M. Ikura and A.M. Gronenborn: Structure of calmodulin-target peptide complexes. Curr. Opinion in Struct. Biol. 3, 838-845 (1993). (207.pdf, 5594905 Bytes)(DOI)
208.
G.M. Clore, A. Bax, J.G. Omichinski and A.M. Gronenborn: Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA. Structure 2, 89-94 (1994). (208.pdf, 678189 Bytes)(DOI)(pubmed)
209.
G. Zhu, D. Live and A. Bax: Analysis of sugar puckers and glycosidic torsion angles in a DNA G-tetrad structure by heteronuclear three-bond J couplings. J. Am. Chem. Soc. 116, 8370-8371 (1994). (209.pdf, 314703 Bytes)(DOI)
210.
A. Bax and S. Grzesiek: Rotating frame Overhauser enhancement spectroscopy. Encyclopedia of Nuclear Magnetic Resonance (D. M. Grant and R. K. Harris, eds), 4157-4167. (210.pdf, 215024 Bytes)
210b.
A. Bax: NMR of ethanol and interferon-g. Encyclopedia of Nuclear Magnetic Resonance (D. M. Grant and R. K. Harris, eds), Vol.1, pp202-207. (210b.pdf, 91073 Bytes)
211.
A. Bax, F. Delaglio, S. Grzesiek and G.W. Vuister: Resonance assignment of methionine methyl groups and c3 angular information from long range proton-carbon J correlation in a calmodulin-peptide complex. J. Biomol. NMR 4, 787-797 (1994). (211.pdf, 813349 Bytes)(DOI)(pubmed)
212.
S. Grzesiek and A. Bax: Interference between dipolar and quadrupolar interactions in the slow tumbling limit: A source of line shift and relaxation in 2H-labeled compounds. J. Am. Chem. Soc. 116, 10196-10201 (1994). (212.pdf, 651039 Bytes)(DOI)
213.
G. Zhu, A. Renwick and A. Bax: Measurement of two-and three-bond 1H-13C J couplings from quantitative J correlation for molecules with overlapping 1H resonance, using t1 noise reduction. J. Magn. Reson. Ser. A 110, 257-261 (1994). (213.pdf, 438912 Bytes)(DOI)
214.
G.W. Vuister, S.-J. Kim, A. Orosz, J. Marquardt, C. Wu and A. Bax: Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nature, Struct. Biol. 1, 605-614 (1994). (214.pdf, 1264065 Bytes)(DOI)(pubmed)
215.
G.W. Vuister, S.-J. Kim, C. Wu and A. Bax: 2D and 3D NMR study of phenylalanine residues in proteins by reverse isotopic labeling. J. Am. Chem. Soc. 116, 9206-9210 (1994). (215.pdf, 647230 Bytes)(DOI)
216.
A. Bax: Multi-dimensional nuclear magnetic resonance methods for protein studies. Curr.. Opinion in Struct. Biol. 4, 738-744 (1994). (216.pdf, 786264 Bytes)(DOI)
217.
A.C. Wang, S. Grzesiek, R. Tschudin, P. J. Lodi and A. Bax: Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N. J. Biomol. NMR, 5, 376-382 (1995). (217.pdf, 564168 Bytes)(DOI)(pubmed)
218.
H. Kuboniwa, S. Grzesiek, F. Delaglio and A. Bax: Measurement of HN-Ha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods.J. Biomol. NMR 4, 871-878 (1994). (218.pdf, 610866 Bytes)(DOI)(pubmed)
219.
A.C. Wang and A. Bax: Reparametrization of the Karplus relation for 3J(HaN) and 3J(HN-C') in peptides from uniformly 13C/15N-enriched human ubiquitin. J. Am. Chem. Soc., 117, 1810-1813 (1995). (219.pdf, 947384 Bytes)(DOI)
220.
S.R. Arepalli, C.P.J. Glaudemans, G.D. Daves Jr., P. Kovac and A. Bax: Identification of protein-mediated indirect NOE effects in a disaccharide-Fab' complex by transferred ROESY. J. Magn. Reson. Ser. B., 106, 195-198 (1995). (220.pdf, 355813 Bytes)(DOI)(pubmed)
221.
L.K. Nicholson, T. Yamazaki, D.A. Torchia, S. Grzesiek, A. Bax, S.J. Stahl, J. D. Kaufman, P.T. Wingfield, P.Y.S. Lam, P.K. Jadhav, C.N. Hodge, P. J. Domaille and C.-H. Chang: Flexibility and function in HIV-1 protease. Nature, Struct. Biol. 2, 274-280 (1995). (221.pdf, 745421 Bytes)(DOI)(pubmed)
222.
S. Grzesiek, H. Kuboniwa, A. Hinck and A. Bax: Multiple-quantum line narrowing for measurement of Ha-Hb J couplings in isotopically enriched proteins. J. Am. Chem. Soc. 117, 5312-5315 (1995). (222.pdf, 1853747 Bytes)(DOI)
223.
S. Grzesiek and A. Bax: Audio-frequency NMR in a nutating frame. Application to the assignment of phenylalanine residues in isotopically labelled proteins. J. Am. Chem. Soc. 117, 6527-6531 (1995). (223.pdf, 610888 Bytes)(DOI)
224.
N. Tjandra, H. Kuboniwa, H. Ren and A. Bax: Rotational dynamics of calcium-free calmodulin studied by 15N NMR relaxation measurements. Eur. J. Biochem. 230, 1014-1024 (1995). (224.pdf, 1248810 Bytes)(DOI)(pubmed)
225.
H. Kuboniwa, N. Tjandra, S. Grzesiek, H. Ren, C.B. Klee and A. Bax: Solution structure of calcium-free calmodulin. Nature, Struct. Biol. 2, 768-776 (1995). (225.pdf, 1180009 Bytes)(DOI)(pubmed)
226.
S. Grzesiek, P. Wingfield, S. Stahl, J. D. Kaufman and A. Bax: Four-dimensional 15N-separated NOESY of slowly tumbling perdeuterated 15N-enriched proteins. Application to HIV-1 nef. J. Am. Chem. Soc. 117, 9594-9595 (1995). (226.pdf, 283591 Bytes)(DOI)
227.
F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax: NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6, 277-293 (1995). (227.pdf, 3747244 Bytes)(DOI)(pubmed)
228.
N. Tjandra, S. E. Feller, R. W. Pastor and A. Bax: Rotational Diffusion Anisotropy of Human Ubiquitin from 15N NMR Relaxation. J. Am. Chem. Soc. 117, 12562-12566 (1995). (228.pdf, 1209625 Bytes)(DOI)
A. Bax, K. Farley and G. S. Walker: Selective HMBC: Increased sensitivity for correlating poorly resolved proton multiplets to carbon-13. J. Magn. Reson. Ser A . 119, 134-138 (1996). (230.pdf, 132108 Bytes)(DOI)
231.
J. Anglister, H. Ren, C. B. Klee and A. Bax: NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide. FEBS Lett. 375, 108-112 (1995). (231.pdf, 447399 Bytes)(DOI)(pubmed)
232.
S. Grzesiek and A. Bax: Spin-locked multiple quantum coherence for signal enhancement in heteronuclear multi-dimensional NMR experiment. J. Biomol. NMR 6, 335-339 (1995). (232.pdf, 447553 Bytes)(DOI)(pubmed)
233.
S. Grzesiek, A. Bax, G. M. Clore, A. M. Gronenborn, J.-S. Hu, J. Kaufman, I. Palmer, S. J. Stahl and P. T. Wingfield: The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nature, Struct. Biol. 3, 340-345 (1996). (233.pdf, 701949 Bytes)(DOI)(pubmed)
234.
S. Grzesiek, S. J. Stahl, P. T. Wingfield, A. Bax: The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. Biochemistry, 35, 10256-10261 (1996). (234.pdf, 379762 Bytes)(DOI)(pubmed)
235.
J.-S. Hu and A. Bax: Measurement of three-bond 13C-13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins. J. Am. Chem. Soc. 118, 8170-8171 (1996). (235.pdf, 112376 Bytes)(235_SI.pdf, 165472 Bytes)(DOI)
236.
N. Tjandra, P. Wingfield, S. Stahl and A. Bax: Anisotropic rotational diffusion of perdeuterated HIV protease from 15N NMR relaxation studies at two fields. J. Biomol. NMR, 8, 273-284 (1996). (236.pdf, 1041602 Bytes)(DOI)(pubmed)
237.
N. Tjandra, S. Grzesiek and A. Bax: Magnetic field dependence of nitrogen-proton J splittings in 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling. J. Am. Chem. Soc. 118, 6264-6272 (1996). (237.pdf, 227000 Bytes)(DOI)
238.
D. Plaksin, S. Chacko, P. McPhie, A. Bax, E. A. Padlan and D. H. Margulies: A T cell receptor Va domain expressed in bacteria: Does it dimerize in solution. J. Exp. Med. 184, 1251-1258, (1996). (238.pdf, 875917 Bytes)(DOI)(pubmed)
239.
N. Tjandra, A. Szabo and A. Bax: Protein backbone dynamics and 15N chemical shift anisotropy from quantitative measurement of relaxation interference. J. Am. Chem. Soc. 118, 6986-6991 (1996). (239.pdf, 218261 Bytes)(DOI)
240.
A. C. LiWang and A. Bax: Equilibrium protium/deuterium fractionation of backbone amides in U-13C/15N labaled human ubiquitin by triple resonance NMR. J. Am. Chem. Soc. 118, 12864-12865 (1996). (240.pdf, 96623 Bytes)(DOI)
J.-S. Hu and A. Bax: chi1 angle information from a simple two-dimensional NMR experiment which identifies trans 3JNCg couplings in isotopically enriched proteins. J. Biomol. NMR. 9, 323-328 (1997). (242.pdf, 96580 Bytes)(DOI)(pubmed)
243.
S. Grzesiek and A. Bax: A three-dimensional NMR experiment with improved sensitivity for carbonyl-carbonyl J correlation in proteins. J. Biomol. NMR. 9, 207-211 (1997). (243.pdf, 108225 Bytes)(DOI)(pubmed)
244.
J.-S. Hu and A. Bax: Determination of phi and chi1 angles in proteins from 13C-13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond? J. Am. Chem. Soc. 119, 6360-6368 (1997). (244.pdf, 252131 Bytes)(DOI)
245.
J.-S. Hu, S. Grzesiek and A. Bax: Two-dimensional NMR methods for determining c1 angles of aromatic residues in proteins from three-bond JC'Cg and JNCgcouplings. J. Am. Chem. Soc. 119, 1803-1804 (1997). (245.pdf, 194677 Bytes)(DOI)
246.
M. Ottiger and A. Bax: An empirical correlation between amide deuterium isotope effects on 13Ca chemical shifts and protein backbone conformation. J. Am. Chem. Soc. 119, 8070-8075 (1997). (246.pdf, 204725 Bytes)(DOI)
247.
N. Tjandra and A. Bax: Measurement of dipolar contributions to 1JCH splittings from magnetic field dependence of J modulation in two-dimensional NMR spectra. J. Magn. Reson. 124, 512-515 (1997). (247.pdf, 152240 Bytes)(DOI)(pubmed)
248.
S. Grzesiek, A. Bax, J.-S. Hu, J. Kaufman, I. Palmer, S. J. Stahl, N. Tjandra and P. T. Wingfield: Refined solution structure and backbone dynamics of HIV-1 Nef. Protein Science, 6, 1248-1263 (1997). (248.pdf, 2767048 Bytes)(DOI)(pubmed)
249.
A. C. LiWang and A. Bax: Solution NMR chracterization of hydrogen bonds by deuterium quadrupole couplings. J. Magn. Reson. 127, 54-64 (1997). (249.pdf, 251936 Bytes)(DOI)(pubmed)
250.
N. Tjandra, J. G. Omichinski, A. M. Gronenbron, G. M. Clore and A. Bax: Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution. Nat. Struct. Biol. 4, 732-738 (1997). (250.pdf, 788511 Bytes)(DOI)(pubmed)
251.
N. Tjandra, D. S. Garrett, A. M. Gronenbron, A. Bax and G. M. Clore: Defining long range order in NMR structure determination dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nat. Struct. Biol. 4, 443-449 (1997). (251.pdf, 838051 Bytes)(DOI)(pubmed)
252.
N. Tjandra and A. Bax: Solution NMR Measurement of amide proton chemical shift anisotropy in 15N-enriched proteins. Correlation with hydrogen bond length. J. Am. Chem. Soc. 119, 8076-8082 (1997). (252.pdf, 233643 Bytes)(DOI)
253.
M. Ottiger, N. Tjandra and A. Bax: Magnetic Field Dependent Amide 15N Chemical Shifts in a Protein-DNA Complex Resulting from Magnetic Ordering in Solution, J. Am. Chem. Soc. 119, 9825-9830 (1997). (253.pdf, 192778 Bytes)(DOI)
254.
N. Tjandra and A. Bax: Large variations in 13Ca chemical shift anisotropy in proteins correlate with secondary structure, J. Am. Chem. Soc. 119, 9576-9577 (1997). (254.pdf, 115225 Bytes)(DOI)
255.
J.-S. Hu and A. Bax: Measurement of three-bond 13C'-13Cb J couplings in human ubiquitin by a triple resonance, E. COSY-type NMR technique, J. Biomol. NMR 11, 199-203 (1998). (255.pdf, 182054 Bytes)(DOI)(pubmed)
256.
A. Bax and N. Tjandra: High resolution NMR of human ubiquitin in an aqueous liquid crystalline medium, J. Biomol. NMR 10, 289-292 (1997). (256.pdf, 171485 Bytes)(DOI)(pubmed)
257.
N. Tjandra and A. Bax: Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science, 278, 1111-1114 (1997). (257.pdf, 346414 Bytes)(DOI)(pubmed)
258.
M. Ottiger, F. Delaglio and A. Bax: Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra, J. Magn. Reson. 131, 373-378 (1998). (258.pdf, 198974 Bytes)(DOI)(pubmed)
259.
G.M. Clore, A.M. Gronenborn and A. Bax: A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J. Magn. Reson. 133, 216-221 (1998). (259.pdf, 234776 Bytes)(DOI)(pubmed)
260.
M. Ottiger and A. Bax: Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules. J. Biomol. NMR 12, 361-372 (1998). (260.pdf, 152927 Bytes)(DOI)(pubmed)
261.
Y.-X. Wang, J.L. Marquardt, P. Wingfield, S.J. Stahl, S. Lee-Huang, D. Torchia and A. Bax: Simultaneous Measurement of 1H-15N, 1H-13C' and 15N-13C' Dipolar Couplings in a Perdeuterated 30 kDa Protein Dissolved in a Dilute Liquid Crystalline Phase. J. Am. Chem. Soc. 120, 7385-7386 (1998). (261.pdf, 46215 Bytes)(DOI)
262.
G.M. Clore, E.C. Murphy, A.M. Gronenborn and A. Bax: Determination of three-bond 1H3'-31P couplings in nucleic acids and protein-nucleic acid complexes by quantitative J correlation spectroscopy. J. Magn. Reson. 134, 164-167 (1998). (262.pdf, 94397 Bytes)(DOI)(pubmed)
263.
G. Cornilescu, J.L. Marquardt, M. Ottiger and A. Bax: Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120, 6836-6837 (1998). (263.pdf, 36489 Bytes)(DOI)
264.
M. Ottiger, F. Delaglio, J.L. Marquardt, N. Tjandra and A. Bax: Measurement of Dipolar Couplings for Methylene and Methyl Sites in Weakly Oriented Macromolecules and their Use in Structure Determination. J. Magn. Reson. 134, 365-369 (1998). (264.pdf, 157003 Bytes)(DOI)(pubmed)
265.
M. Ottiger and A. Bax: Determination of Relative N-HN, N-C', Ca-C' and Ca-Ha effective bond lengths in a protein by NMR in a dilute liquid crystalline phase. J. Am. Chem. Soc. 120, 12334-12341 (1998). (265.pdf, 106321 Bytes)(DOI)
266.
C.A. Bewley, K.R. Gustafson, M.R. Boyd, D.G. Covell, A. Bax, G.M. Clore and A.M. Gronenborn: Solution structure of cyanovirin-N, a potent HIV-inactivating protein from the cyanobacterium Nostoc ellipsosporum. Nature, Struct. Biol. 5, 571-578 (1998). (266.pdf, 758248 Bytes)(DOI)(pubmed)
267.
B.E. Ramirez and A. Bax: Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium. J. Am. Chem. Soc. 120, 9106-9107 (1998). (267.pdf, 35840 Bytes)(DOI)
268.
J.L. Markley, A. Bax, Y. Arata, C.W. Hilbers, R. Kaptein, B.D. Sykes, P.E. Wright and K. Wüthrich: Recommendations for the presentation of NMR structures of proteins and nucleic acids. Pure and Appl. Chem. 70, 117-142 (1998). (268.pdf, 1950531 Bytes)(DOI)
269.
M. Ottiger and A. Bax: Bicelle-based liquid crystals for NMR-measurement of Dipolar couplings at acidic and basic pH values. J. Biomol. NMR, 13, 187-191 (1999). (269.pdf, 63709 Bytes)(DOI)(pubmed)
270.
B.W. Koenig, J.-S. Hu, M. Ottiger, S. Bose, R.W. Hendler and Ad Bax: NMR Measurement of dipolar couplings in proteins aligned by transient binding to purple membrane fragments. J. Am. Chem. Soc. 121, 1385-1386 (1999). (270.pdf, 40067 Bytes)(DOI)
271.
S. Gaemers, C.J. Elsevier and A. Bax: NMR of biomolecules in low viscosity, liquid CO2. Chem. Phys. Lett. 301, 138-144 (1999). (271.pdf, 234459 Bytes)(DOI)
272.
G. Cornilescu, F. Delaglio and A. Bax: Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR, 13, 289-302 (1999). (272.pdf, 175833 Bytes)(DOI)(pubmed)
273.
G. Cornilescu, J.-S. Hu and A. Bax: Identification of the hydrogen bonding network in a protein by scalar couplings. J. Am. Chem. Soc. 121, 2949-2950 (1999). (273.pdf, 44063 Bytes)(DOI)
274.
G. Cornilescu, B.E. Ramirez, M.K. Frank, G.M. Clore, A.M. Gronenborn and A. Bax: Correlation between 3hJNC' and hydrogen bond length in proteins. J. Am. Chem. Soc. 121, 6275-6279 (1999). (274.pdf, 81625 Bytes)(DOI)
275.
Y.-X. Wang, J. Jacob, F. Cordier, P. Wingfield, S.J. Stahl, S. Lee-Huang, D.A. Torchia, S. Grzesiek and A. Bax: Measurement of 3hJNC' connectivities across hydrogen bonds in a 30 kDa protein. J. Biomol. NMR, 14, 181-184 (1999). (275.pdf, 67197 Bytes)(DOI)(pubmed)
276.
M. Ottiger and A. Bax: How tetrahedral are methyl groups in proteins? A liquid crystal NMR study. J. Am. Chem. Soc. 121, 4690-4695 (1999). (276.pdf, 87870 Bytes)(DOI)
277.
F. Cordier, M. Rogowski, S. Grzesiek, and A. Bax: Observation of through-hydrogen-bond (2h)J(HC') in a perdeuterated protein. J. Magn. Reson. 140, 510-512 (1999). (277.pdf, 59000 Bytes)(DOI)(pubmed)
278.
G. Kontaxis, G.M. Clore, and A. Bax: Evaluation of cross correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J. Magn. Reson. 143, 184-196 (2000). (278.pdf, 199604 Bytes)(DOI)(pubmed)
279.
Y.-X. Wang, N. Neamati, J. Jacob, I. Palmer, S.J. Stahl, J.D. Kaufman, P. Lin Huang, P. Lee Huang, H.E. Winslow, Y. Pommier, P.T. Wingfield, S. Lee-Huang, A. Bax, and D.A. Torchia: Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions. Cell 99, 433-442 (1999). (279.pdf, 370136 Bytes)(DOI)(pubmed)
280.
G. Cornilescu, A. Bax, and D. Case: Large variations in one-bond (13)C(alpha)-(13)C(beta) J couplings in polypeptides correlate with backbone conformation. J. Am. Chem. Soc. 122, 2168-2171 (2000). (280.pdf, 90178 Bytes)(DOI)
281.
B. Koenig, D. C. Mitchell, S. König, S. Grzesiek, B.J. Litman, and A. Bax: Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin. J. Biomol. NMR. 16, 121-125 (2000). (281.pdf, 62289 Bytes)(DOI)(pubmed)
282.
F. Delaglio, G. Kontaxis, and A. Bax: Protein structure determination using molecular fragment replacement and NMR dipolar couplings, J. Am. Chem. Soc. 122, 2142-2143 (2000). (282.pdf, 78521 Bytes)(DOI)
283.
M. Zweckstetter and A. Bax: Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR, J. Am. Chem. Soc., 122, 3791-3792 (2000). (283.pdf, 32037 Bytes)(DOI)
284.
N. Tjandra, S. Tate, A. Ono, M. Kainosho, and A. Bax: The NMR structure of a DNA dodecamer in an aqueous dilute liquid crystalline phase. J. Am. Chem. Soc., 122, 6190-6200 (2000). (284.pdf, 314112 Bytes)(DOI)
285.
B.E. Ramirez, O.N. Voloshin, R.D. Camerini-Otero, and A. Bax: Solution structure of DinI provides insight into its mode or RecA inactivation. Protein Science, 9, 2161-2169 (2000). (285.pdf, 1363517 Bytes)(DOI)(pubmed)
286.
J.J. Chou, F. Delaglio, and A. Bax: Measurement of 15N-13C' dipolar couplings in medium sized proteins. J. Biomol. NMR, 18, 101-105 (2000). (286.pdf, 62223 Bytes)(DOI)(pubmed)
287.
J.J. Chou, S. Li, and A. Bax: Study of conformational rearrangement and refinement of homology models by the use of heteronuclear dipolar couplings. J. Biomol. NMR, 18, 217-227 (2000). (287.pdf, 178350 Bytes)(DOI)(pubmed)
288.
G. Cornilescu and A. Bax: Measurement of proton, nitrogen and carbonyl chemical shielding anisotropies in a protein dissolved in a dilute liquid crystalline phase. J. Am. Chem. Soc. 122, 10143-10154 (2000). (288.pdf, 156433 Bytes)(DOI)
289.
A. Bax, G. Kontaxis and N. Tjandra: Dipolar couplings in macromolecular structure determination, Meth. Enzymol. 339, 127-174 (2001). (289.pdf, 4233490 Bytes)(DOI)(pubmed)
290.
Z. Wu and A. Bax: Measurement of homonuclear proton couplings based on cross-peak nulling in CT-COSY. J. Magn. Reson., 151, 242-252 (2001). (290.pdf, 437289 Bytes)(DOI)(pubmed)
291.
Z. Wu, A. Ono, M. Kainosho, and A. Bax: H...N hydrogen bond lengths in double stranded DNA from internucleotide dipolar couplings, J. Biomol. NMR 19, 361-365 (2001). (291.pdf, 67051 Bytes)(DOI)(pubmed)
292.
F. Delaglio, Z. Wu and A. Bax: Measurement of homonuclear proton couplings from regular 2D COSY spectra, J. Magn. Reson. 149, 276-281 (2001). (292.pdf, 215764 Bytes)(DOI)(pubmed)
293.
Z. Wu, N. Tjandra, and A. Bax: Measurement of 1H3'-31P dipolar couplings in a DNA oligonucleotide by constant-time NOESY difference spectroscopy. J. Biomol. NMR 19, 367-370 (2001). (293.pdf, 56389 Bytes)(DOI)(pubmed)
294.
Z. Wu, N. Tjandra, and A. Bax: 31P chemical shift anisotropy as an aid in determining nucleic acid structure in liquid crystals. J. Am. Chem. Soc. 123, 3617-3618 (2001). (294.pdf, 44852 Bytes)(DOI)(pubmed)
295.
J.J. Chou and A. Bax: Protein sidechain rotamers from dipolar couplings in a liquid crystalline phase. J. Am. Chem. Soc. 123, 3844-3845 (2001). (295.pdf, 42447 Bytes)(DOI)(pubmed)
296.
G. Kontaxis and A. Bax: Multiplet component separation for measurement of methyl 13C-1H dipolar couplings in weakly aligned proteins. J. Biomol. NMR 20, 77-82 (2001). (296.pdf, 147597 Bytes)(DOI)(pubmed)
297.
M. Zweckstetter and A. Bax: Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage. J. Biomol. NMR, 20, 365-377 (2001). (297.pdf, 177259 Bytes)(DOI)(pubmed)
298.
O.N. Voloshin, B.E. Ramirez, A. Bax, and R.D. Camerini-Otero: A model for the abrogation of the SOS response by an SOS protein: a negatively charged helix in DinI mimics DNA in its interaction with RecA. Gene Dev. 15: 415-427 (2001). (298.pdf, 825065 Bytes)(DOI)(pubmed)
299.
M. Zweckstetter and A. Bax: Single-step determination of protein substructures using dipolar couplings: Aid to structural genomics. J. Am. Chem. Soc. 123, 9490-9491 (2001). (299.pdf, 45970 Bytes)(299_SI.pdf, 78482)(DOI)(pubmed)
300.
J.J. Chou, S.P. Li, C.B. Klee, and A. Bax: Solution structure of Ca2+-calmodulin reveals flexible hand-like properties of its domains. Nature Struct. Biol. 8, 990-997 (2001). (300.pdf, 2035940 Bytes)(DOI)(pubmed)
301.
S. Gaemers and A. Bax: Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy, J. Am. Chem. Soc. 123, 12343-12352 (2001). (301.pdf, 120946 Bytes)(DOI)(pubmed)
302.
J.J. Chou, S. Gaemers, B. Howder, J.M. Louis, and A. Bax: A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J. Biomol. NMR, 21, 377-382 (2001). (302.pdf, 116030 Bytes)(DOI)(pubmed)
303.
J.J. Chou, J.D. Kaufman, S.J. Stahl, P.T. Wingfield, and A. Bax: Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in a stretched polyacrylamide gel. J. Am. Chem. Soc. 124, 2450-2451 (2002). (303.pdf, 124979 Bytes)(DOI)(pubmed)
304.
A. Bax, J.J. Chou, and B. Ramirez: Liquid Crystalline Samples: Maromolecular Structure Determination. Encyclopedia of Nuclear Magnetic Resonance, Encyclopedia of Nuclear Magnetic Resonance (D. M. Grant and R. K. Harris, eds), Vol.9, 401-412. (304.pdf, 208661 Bytes)
305.
B.W. Koenig, G. Kontaxis, D.C. Mitchell, J.M. Louis, B.J. Litman, A. Bax: Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings. J. Mol. Biol. 322, 441-461 (2002). (305.pdf, 1330109 Bytes)(DOI)(pubmed)
306.
J. Boisbouvier and A. Bax: Long-range magnetization transfer between uncoupled nuclei by dipole-dipole cross-correlated relaxation: A precise probe of beta-sheet geometry in proteins. J. Am. Chem. Soc. 124, 11038-11045 (2002). (306.pdf, 173636 Bytes)(DOI)(pubmed)
307.
Z. Wu and A. Bax: Measurement of long-range 1H-1H dipolar couplings in weakly aligned proteins. J. Am. Chem. Soc. 124, 9672-9673 (2002). (307.pdf, 58168 Bytes)(DOI)(pubmed)
308.
M. Zweckstetter and A. Bax: Evaluation of uncertainty in alignment tensors obtained from dipolar couplings. J. Biomol. NMR 23,127-137 (2002). (308.pdf, 218355 Bytes)(DOI)(pubmed)
309.
A. Bax: Weak alignment offers new NMR opportunities to study protein structure and dynamics. Prot. Science, 12, 1-16 (2003). (309.pdf, 360876 Bytes)(DOI)(pubmed)
310.
J.A. Lukin, G. Kontaxis, V. Simplaceanu, Y. Yuan, A. Bax, C. Ho: Quaternary structure of hemoglobin in solution. Proc. Natl. Acad. Sci. 100, 517-520 (2003). (310.pdf, 250422 Bytes)(DOI)(pubmed)
311.
J. Boisbouvier, F. Delaglio, and A. Bax: Direct observation of dipolar couplings between distant protons in weakly aligned nucleic acids Proc. Natl. Acad. Sci. 100, 11333-11338 (2003). (311.pdf, 504105 Bytes)(DOI)(pubmed)
312.
T.S. Ulmer, S. Soelaiman, S.P. Li , C.B. Klee, W.J. Tang, and A. Bax: Calcium dependence of the interaction between calmodulin and anthrax edema factor. J. Biol. Chem. 278, 29261-29266 (2003). (312.pdf, 502751 Bytes)(DOI)(pubmed)
T.S. Ulmer, B.E. Ramirez, F. Delaglio, and A. Bax: Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J. Am. Chem. Soc. 125, 9179-9191 (2003). (314.pdf, 640837 Bytes)(314_SI.pdf, 829835 Bytes)(DOI)(pubmed)
315.
J. Boisbouvier, Z. Wu, A. Ono, M. Kainosho, and A. Bax: Rotational diffusion tensor of nucleic acids from C-13 NMR relaxation. J. Biomol. NMR 27, 133-142 (2003). (315.pdf, 150216 Bytes)(DOI)(pubmed)
316.
A.A. Gakh, A.Y. Romanovich, and A. Bax: Thermodynamic rearrangement synthesis and NMR structures of C-1, C-3, and T isomers of C60H36. J. Am. Chem. Soc. 125, 7902-7906 (2003). (316.pdf, 237550 Bytes)(DOI)(pubmed)
317.
Z. Wu, F. Delaglio, N. Tjandra, V.B. Zhurkin, and A. Bax : Overall structure and sugar dynamics of a DNA dodecamer from homoand heteronuclear dipolar couplings and P-31 chemical shift anisotropy. J. Biomol. NMR 26, 297-315 (2003). (317.pdf, 397981 Bytes)(DOI)(pubmed)
J.A. Lukin, G. Kontaxis, V. Simplaceanu, Y. Yuan , A. Bax, and C. Ho: Backbone resonance assignments of human adult hemoglobin in the carbonmonoxy form, J. Biomol. NMR 28, 203-204 (2004). (319.pdf, 120575 Bytes)(DOI)(pubmed)
320.
D.L. Bryce and A. Bax: Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids. J. Biomol. NMR 28, 273-287 (2004). (320.pdf, 436936 Bytes)(DOI)(pubmed)
J.J. Chou, J.L. Baber and A. Bax: Characterization of phospholipid mixed micelles by translational diffusion, J. Biomol. NMR 29, 299-308 (2004). (322.pdf, 171791 Bytes)(DOI)(pubmed)
323.
M. Zweckstetter, G. Hummer and A. Bax: Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases. Biophys. J. 86, 3444-3460 (2004). (323.pdf, 313319 Bytes)(DOI)(pubmed)
324.
C.P. Jaroniec, T.S. Ulmer and A. Bax: Quantitative J correlation methods for the accurate measurement of 13C'-13CA dipolar couplings in proteins. J. Biomol. NMR 30, 181-194 (2004). (324.pdf, 608220 Bytes)(DOI)(pubmed)
325.
D.L. Bryce, J. Boisbouvier, and A. Bax: Experimental and Theoretical Determination of Nucleic Acid Magnetic Susceptibility: Importance for the Study of Dynamics by Field-Induced Residual Dipolar Couplings. J. Am. Chem. Soc. 126, 10820-10821 (2004). (325.pdf, 67826 Bytes)(325-supportinfo.pdf, 521722 Bytes)(DOI)(pubmed)
326.
E. Miclet, D.C. Williams Jr., G. M. Clore, D.L. Bryce, J. Boisbouvier and A. Bax: Relaxation-Optimized NMR Spectroscopy of Methylene Groups in Proteins and Nucleic Acids. J. Am. Chem. Soc. 126, 10560-10570 (2004). (326.pdf, 233025 Bytes)(326-supportinfo.pdf, 253029 Bytes)(DOI)(pubmed)
327.
G. Kontaxis, F. Delaglio and A. Bax: Molecular fragment replacement approach to protein structure determination by chemical shift and dipolar homology database mining. Meth. Enzymol. 394, 42-78 (2005). (327.pdf, 820275 Bytes)(DOI)(pubmed)
328.
E. O'Neil-Cabello, Z. Wu, D.L. Bryce, E.P. Nikonowicz, and A. Bax: Enhanced spectral resolution in RNA HCP spectra for measurement of 3JC2'P and 3JC4'P couplings and 31P chemical shift changes upon weak alignment. J. Biomol. NMR 30, 61-70 (2004). (328.pdf, 335310 Bytes)(DOI)(pubmed)
J. Boisbouvier, D.L. Bryce, E. O'Neil-Cabello, E.P. Nikonowicz, and A. Bax: Resolution-optimized NMR measurement of 1DCH, 1DCC and 2DCH residual dipolar couplings in nucleic acid bases. J. Biomol. NMR 30, 287-301 (2004). (330.pdf, 621309 Bytes)(330-supportinfo.pdf, 232309 Bytes)(DOI)(pubmed)
331.
Z. Wu, M. Maderia, J.J. Barchi Jr, V.E. Marquez and A. Bax: Changes in DNA-bending induced by restricting nucleoside ring pucker studied by weak alignment NMR spectroscopy. Proc. Natl. Acad. Sci. USA 102, 24-28 (2005). (331.pdf, 320133 Bytes)(DOI)(pubmed)
A. Grishaev and A. Bax: Weak alignment NMR: a hawk-eyed view of biomolecular structure. Cur. Opinion Struct. Biol. 15, 563-570 (2005). (335.pdf, 225761 Bytes)(DOI)(pubmed)
M.M. Pierce, U. Baxa, A.C. Steven, A. Bax, and R.B. Wickner: Is the prion domain of soluble Ure2p unstructured? Biochemistry, 44, 321-328 (2005). (337.pdf, 284557 Bytes)(DOI)(pubmed)
338.
M. Maderia M, J. Wu, A. Bax, S. Shenoy, B. O'Keefe, V.E. Marquez, and J.J. Barchi: Engineering DNA topology with locked nucleosides: A structural study. Nucleosides, nucleotides & nucleic acids, 24, 687-690 (2005).(338.pdf, 290842 Bytes)(DOI)(pubmed)
Z. Wu, F. Delaglio, K. Wyatt, G. Wistow, and A. Bax: Solution structure of gS crystallin by molecular fragment replacement NMR, Prot. Sci. 14, 3101-3114 (2005). (340.pdf, 556461 Bytes)(DOI)(pubmed)
341.
C.P. Jaroniec, J. D. Kaufman, S.J. Stahl, M. Viard, R. Blumenthal, P. T. Wingfield, and A. Bax: Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain. Biochemistry, 44, 16167-16180 (2005). (341.pdf, 625073 Bytes)(341-supportinfo.pdf, 398102 Bytes)(DOI)(pubmed)
J. Ying, A. Grishaev, and A. Bax: Carbon chemical shift anisotropy in DNA bases from field dependence of NMR relaxation rates. Magn. Reson. Chem., 44, 302-310 (2006).(343.pdf, 252215 Bytes)(pubmed)
344.
J.H. Chill, J.M. Louis, C. Miller, and A. Bax: NMR study of the tetrameric KcsA potassium channel in detergent micelles. Prot. Sci. 15, 684-698 (2006). (344.pdf, 678376 Bytes)(DOI)(pubmed)
345.
J. Dam, J. Baber, A. Grishaev, E.L. Malchiodi, P. Schuck, A. Bax, and R.A. Mariuzza: Variable Dimerization of the Ly49A Natural Killer Cell Receptor Results in Differential Engagement of its MHC Class I Ligand. J. Mol. Biol. 362, 102-113 (2006). (345.pdf, 660278 Bytes)(DOI)(pubmed)
346.
J. Ying, A. Grishaev, D.L. Bryce, and A. Bax: Chemical Shift Tensors of Protonated Base Carbons in Helical RNA from NMR Relaxation and Liquid Crystal Measurements. J. Am. Chem. Soc. 128, 11443-11454 (2006). (346.pdf, 345403 Bytes)(DOI)(pubmed)
J.H. Chill, J.M. Louis, J.L. Baber, and A. Bax: Measurement of 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel. J. Biomol. NMR, 36, 123-136 (2006). (349.pdf, 426461 Bytes)(DOI)(pubmed)
J. Ying, Alexander Grishaev, M.P. Latham, A. Pardi, and A. Bax: Magnetic field induced residual dipolar couplings of imino groups in nucleic acids from measurements at a single magnetic field. J. Biomol. NMR, 39, 91-96 (2007). (354.pdf, 249801 Bytes)(354-supportinfo.pdf, 280836 Bytes)(DOI)(pubmed)
Y. Shen, O. Lange, F. Delaglio, P. Rossi, J.M. Aramini, G. Liu, A. Eletsky, Y. Wu, K.K. Singarapu, A. Lemak, A. Ignatchenko, C.H. Arrowsmith, T. Szyperski, G.T. Montelione, D. Baker, and A. Bax: Consistent blind protein structure generation from NMR chemical shift data. Proc. Natl. Acad. Sci. USA 105, 4685-4690 (2008). (359.pdf, 1126804 Bytes)(359_Support_Info.pdf, 1088310 Bytes)(DOI)(pubmed)
360.
L.M. Parsons, A. Grishaev, and A. Bax: The periplasmic domain of TolR forms a large hydrophobic groove and may contact TolQ through its C-terminus: NMR solution structure and comparison to SAXS data. Biochemistry, 47, 3131-3142 (2008). (360.pdf, 2607243 Bytes)(360_Support_Info.pdf, 477910 Bytes)(DOI)(pubmed)
361.
J. Lorieau, L. Yao, and A. Bax: Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins. J. Am. Chem. Soc., 130, 7536-7537 (2008). (361.pdf, 344676 Bytes)(361_Support_Info.pdf, 1268622 Bytes)(dGpG Protocol, 80651 Bytes)(Company for the material : Yogesh Sanghvi; rasayan@sbclocal.net; Phone: 760-944-1541; Fax: 760-944-1543; Rasayan Inc., 2802 Crystal Ridge Road Encinitas, CA 92024-6615 U.S.A.) (DOI)(pubmed)
R.B. Best, K.A. Merchant, I.V. Gopich, B. Schuler, A. Bax, and W.A. Eaton: Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. Proc. Natl. Acad. Sci. USA 104, 18964-18969 (2007).(364.pdf, 740015 Bytes)(pubmed)
365.
A. Grishaev, V. Tugarinov, L.E. Kay, J. Trewhella, and A. Bax: Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. J. Biomol. NMR 40, 95-106 (2008). (365.pdf, 435099Bytes)(365-supportinfo.pdf, 227933Bytes)(DOI)(pubmed)
A. Grishaev, J. Ying, M. D. Canny, A. Pardi, and A. Bax: Solution structure of tRNA(Val) from refinement of homology model against residual dipolar coupling and SAXS data, J. Biomol. NMR 42, 99-109 (2008). (367.pdf, 377315)(367-supportinfo.pdf, 35823)(DOI)(pubmed)
368.
A. Grishaev, L.S. Yao, J.F. Ying, A. Pardi, and A. Bax: Chemical shift anisotropy of imino 15N nuclei in Watson-Crick basepairs from magic angle liquid crystal NMR and nuclear spin relaxation. J. Am. Chem. Soc. 131, 9490-9491 (2009). (368.pdf, 365114)(368-supportinfo.pdf, 220417)(DOI)(pubmed)
Y. Shen, P.N. Bryan, Y. He, J. Orban, D. Baker, and A. Bax: De novo structure generation using chemical shifts for proteins with high sequence identity but different folds. Protein Sci. 19, 349-356 (2010). (371.pdf, 653334)(371-supportinfo.pdf, 621016)(DOI)(pubmed)
L. Yao, A. Grishaev, G. Cornilescu, and A. Bax: Site-specific N-15 chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements. J. Am. Chem. Soc. 132, 4295-4309 (2010). (373.pdf, 883041)(373-supportinfo.pdf, 620976)(DOI)(pubmed)
374.
C.R. Bodner, A.S. Maltsev, C.M. Dobson, and A. Bax: Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy. Biochemistry, 49, 862-871 (2010). (374.pdf, 3492555)(374-supportinfo.pdf, 340006)(DOI)(pubmed)
B.S. Tolbert, Y. Miyazaki, S. Barton, B. Kinde, P. Starck, R. Singh, A. Bax, D.A. Case, and M.F. Summers: Major groove width variations in RNA structures determined by NMR and impact of C-13 residual chemical shift anisotropy and H-1-C-13 residual dipolar coupling on refinement. J. Biomol. NMR, 47, 205-19 (2010) (376.pdf, 1036202)(DOI)(pubmed)
377.
J.L. Lorieau, J.M. Louis, and A. Bax: The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface. Proc. Natl. Acad. Sci. USA 107, 11341-11346 (2010) (377.pdf, 1197845)(377_SI.pdf, 1567419)(DOI)(pubmed)
378.
L. Yao, A. Grishaev, G. Cornilescu, and Ad Bax: The Impact of Hydrogen Bonding on Amide 1H Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy. J. Am. Chem. Soc. 132, 10866-10875 (2010) (378.pdf, 1553724)(378_SI.pdf, 523360)(DOI)(pubmed)
379.
Y. Shen and A. Bax: SPARTA+: a modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network. J. Biomol. NMR 48, 13-22 (2010). (379.pdf, 488635)(379_SI.pdf, 239288)(DOI)(pubmed)
A. Grishaev, L.A. Guo, T. Irving, and A. Bax: Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling. J. Am. Chem. Soc. 132, 15484-15486 (2010) (381.pdf, 739489)(381_supportinfo.pdf, 412734)(DOI)(pubmed)
J.L. Lorieau, J.M. Louis, and A. Bax: Helical Hairpin Structure of Influenza Hemagglutinin Fusion Peptide Stabilized by Charge-Dipole Interactions between the N-terminal Amino Group and the Second Helix. J. Am. Chem. Soc. 133, 2824-2827 (2011). (383.pdf, 1337185)(383_SI.pdf, 135630)(DOI)(pubmed)
384.
J. Ying, J. Wang, A. Grishaev, P. Yu, Y.X. Wang, and A. Bax: Measurement of 1H-15N and 1H-13C residual dipolar couplings in nucleic acids from TROSY intensities. J. Biomol. NMR 51, 89-103 (2011). (384.pdf, 2288375)(384_supportinfo.pdf, 440915)(DOI)(pubmed)
385.
P. Trigo-Mourino, A. Navarro-Vazquez, J. Ying, R.R. Gil, and A. Bax: Structural Discrimination in Small Molecules by Accurate Measurement of Long-Range Proton-Carbon NMR Residual Dipolar Couplings. Angew. Chem. Int. Ed. 50, 7576-7580 (2011). (385.pdf, 771827)(385_SI.pdf, 1747470)(DOI)(pubmed)
N.G. Sgourakis, O.F. Lange, F. DiMaio, I. Andre, N.C. Fitzkee, P. Rossi, G.T. Montelione, A. Bax, and D. Baker: Determination of the Structures of Symmetric Protein Oligomers from NMR Chemical Shifts and Residual Dipolar Couplings. J. Am. Chem. Soc. 133, 6288-6298 (2011). (387.pdf, 3995149)(387_SI.pdf, 4496613)(DOI)(pubmed)
J.L. Lorieau, J.M. Louis, and A. Bax: Whole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxation. J. Am. Chem. Soc. 133, 14184-14187 (2011). (389.pdf, 1490981)(389_SI.pdf, 453484)(DOI)(pubmed)
390.
A. Grishaev, J. Ying, and A. Bax: Imino Hydrogen Positions in Nucleic Acids from Density Functional Theory Validated by NMR Residual Dipolar Couplings. J. Am. Chem. Soc. 134, 6956-6959 (2012). (390.pdf, 412954)(390_SI.pdf, 228832)(DOI)(pubmed)
391.
J.L. Lorieau, J. Louis, and A. Bax: The Impact of Influenza Hemagglutinin Fusion Peptide Length and Viral Subtype on its Structure and Dynamics. Biopolymers 99, 189-195 (2013). (391.pdf, 496546)(391_SI.pdf, 92473)(DOI)(pubmed)
392.
A.S. Maltsev, J. Ying, and A. Bax: Impact of N-terminal Acetylation of a-Synuclein on its Random Coil and Lipid Binding Properties. Biochemistry (Accelerated Publication) 51, 5004-5013 (2012). (392.pdf, 1140392)(392_SI.pdf, 649335)(DOI)(pubmed)
393.
N. Lakomek, J. Ying, and A. Bax: Measurement of (15)N relaxation rates in perdeuterated proteins by TROSY-based methods. J. Biomol. NMR 53, 209-221 (2012). (393.pdf, 698239)(393_SI.pdf, 606611)(DOI)(pubmed)
394.
J. L. Lorieau, J.M. Louis, C.D. Schwieters and A. Bax: pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR. Proc. Natl. Acad. Sci. USA, 109, 19994-19999 (2012). (394.pdf, 540486)(394_SI.pdf, 451389)(DOI)(pubmed)
395.
A.S. Maltsev, J. Ying, and A. Bax: Deuterium isotope shifts for backbone H-1, N-15 and C-13 nuclei in intrinsically disordered protein α-synuclein. J. Biomol. NMR. 54, 181-191 (2012). (395.pdf, 416705)(395_SI.pdf, 136380)(DOI)(pubmed)
396.
N.A. Lakomek, J.D. Kaufman, S.J. Stahl, J.M. Louis, A. Grishaev, P.T. Wingfield, and A. Bax: The homotrimeric HIV-1 viral coat protein gp41 shows a high degree of internal dynamics on multiple time scales. Angew. Chem. Intl. Engl. Ed. 52, 3911-3915 (2013). (396.pdf, 1025300)(396_SI.pdf, 1156218)(DOI)(pubmed)
397.
A.S. Maltsev, J. Chen, R.L. Levine, and A. Bax: Site-specific interaction between α-synuclein and membranes probed by NMR-observed methionine oxidation rates J. Am. Chem. Soc. 135, 2943-2946 (2013). (397.pdf, 637143)(397_SI.pdf, 500894)(DOI)(pubmed)
398.
Y. Shen and A. Bax: Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J. Biomol. NMR. 56, 227-241 (2013). (398.pdf, 805365)(398_SI.pdf, 1064628)(DOI)(pubmed)
399.
J.L. Lorieau, A.S. Maltsev, J.M. Louis, and A. Bax: Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles. J. Biomol. NMR. 55, 369-377 (2013). (399.pdf, 308295)(399_SI.pdf, 205983)(DOI)(pubmed)
400.
J. Roche, J. Ying, A. S. Maltsev and A. Bax: Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of a-synuclein. ChemBiochem, 14, 1754-1761. (400.pdf, 1224755)(400_SI.pdf, 297211)(DOI)(pubmed)
401.
J. Roche, J.M. Louis, A. Grishaev, J. Ying, and A. Bax: Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion, Proc. Nat. Acad. Sci. USA 111, 3425-3430 (2014). (401.pdf, 1856373)(DOI)(pubmed)
402.
A.S. Maltsev, A. Grishaev, J. Roche, M. Zasloff, and A. Bax: Improved cross validation of a static ubiquitin structure derived from high precision residual dipolar couplings measured in a drug-based liquid crystalline phase. J. Am. Chem. Soc. 136, 3752-3755 (2014). (402.pdf, 1006270)(402_SI.pdf, 436648)(DOI)(pubmed)
403.
J. Ying, J. Roche, and A. Bax: Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins. J. Magn. Reson. 241, 97-102 (2014). (403.pdf, 966992)(403_SI.pdf, 49630)(DOI)(pubmed)
404.
N.G. Sgourakis, K.Natarajan, J. Ying, B. Vogeli, L.F Boyd, D.H, Margulies, A. Bax: The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family. Structure 22, 1-11 (2014). (404.pdf, 2813452)(404_SI.pdf, 938068)(DOI)(pubmed)
405.
A.B. Mantsyzov, A.S. Maltsev, J.Ying, Y. Shen, G. Hummer, A. Bax: A maximum entropy approach to the study of residue-specific backbone angle distributions in a-synuclein, an intrinsically disordered protein. Prot. Science 23, 1275-1290 (2014). (405.pdf, 695775)(405_SI.pdf, 1196343)(DOI)(pubmed)
406.
A.B. Hickman, H.E. Hosam, X.H. Li, J.A. Knapp, T. Laver, A.L. Dos, G. Tolun, A.C. Steven, A. Grishaev, A. Bax, P.W. Atkinson, N.L. Craig, and F. Dyda: Structural Basis of hAT Transposon End Recognition by Hermes, an Octameric DNA Transposase from Musca domestica. Cell 158, 353-367 (2014). (406.pdf, 4498328)(DOI)(pubmed)
407.
J. Ying, F. Li, J.H. Lee, and A. Bax: 13Calpha decoupling during direct observation of carbonyl resonances in solution NMR of isotopically enriched proteins. J. Biomol. NMR 60, 15-21 (2014). (407.pdf, 724858)(407_SI.pdf, 181067)(DOI)(pubmed)
408.
L.Y. An, Y.F. Wang, N. Zhang, S.H. Yan, Bax, A. and L.S. Yao: Protein Apparent Dielectric Constant and Its Temperature Dependence from Remote Chemical Shift Effects J. Am. Chem. Soc. 136, 12816-12819 (2014). (408.pdf, 1727309)(408_SI.pdf, 388359)(DOI)(pubmed)
409.
F. Li, J.H. Lee, A. Grishaev, J. Ying, and A. Bax: High Accuracy of Karplus Equations for Relating Three-Bond J Couplings to Protein Backbone Torsion Angles, ChemPhysChem (2015). (409.pdf, 812981)(409_SI.pdf, 257973)(DOI)(pubmed)
410.
Y. Shen and A. Bax: Protein Structural Information Derived from NMR Chemical Shift with the Neural Network Program TALOS-N, Methods Mol. Biol. 1260: 17-32 (2015). (410.pdf, 479703)(DOI)(pubmed)
411.
J.H. Lee, F. Li, A. Grishaev, and A. Bax: Quantitative Residue-specific Protein Backbone Torsion Angle Dynamics from Concerted Measurement of (3)J Couplings, J. Am. Chem. Soc. 137, 1432-1435 (2015). (411.pdf, 1156313)(411_SI.pdf, 613369)(DOI)(pubmed)
412.
J. Roche, J.M. Louis, and A. Bax: Conformation of Inhibitor-Free HIV-1 Protease Derived from NMR Spectroscopy in a Weakly Oriented Solution, ChemBioChem 16, 214-218 (2015). (412.pdf, 1355627)(412_SI.pdf, 76784)(DOI)(pubmed)
413.
G.T. Montelione, M. Nilges, A. Bax, P. Güntert, T. Herrmann, J.S. Richardson, C. Schwieters, W.F. Vranken, G.W. Vuister, D.S. Wishart, H.M. Berman, G.J. Kleywegt, and J.L. Markley: Recommendations of the wwPDB NMR Validation Task Force, Structure 21, 1563-1570 (2013) (413.pdf, 221817)(DOI)(pubmed)
414.
J. Roche, J.M. Louis, A. Aniana, R. Ghirlando, and A. Bax: Complete Dissociation of the HIV-1 gp41 Ectodomain and Membrane Proximal Regions upon Phospholipid Binding, J. Biomol. NMR. 61, 235-248 (2015). (414.pdf, 1871225)(414_SI.pdf, 307598)(DOI)(pubmed)
A.B. Mantsyzov, Y. Shen, J.H. Lee, G. Hummer, and A. Bax: MERA: a Webserver for Evaluating Backbone Torsion Angle Distributions in Dynamic and Disordered Proteins from NMR Data, J. Biomol. NMR. 63, 85-95 (2015). (416.pdf, 1496412)(DOI)(pubmed)
417.
F. Li, A. Grishaev, J. Ying, and A. Bax: Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings, J. Am. Chem. Soc. 137, 14798-14811 (2015). (417.pdf, 1686883)(417_SI.pdf, 963132)(DOI)(pubmed)
418.
N.G. Sgourakis, N.A. May, L.F. Boyd, J. Ying, A. Bax, D.H. Margulies: A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR, J. Biol. Chem. 290, 28857-28868 (2015). (418.pdf, 3084619)(DOI)(pubmed)
419.
J. Roche, J.M. Louis, A. Bax, R.B. Best: Pressure-induced Structural Transition of Mature HIV-1 Protease from a Combined NMR/MD Simulation Approach, Proteins 83, 2117-2123 (2015). (419.pdf, 360737)(419_SI.pdf, 2424491)(DOI)(pubmed)
420.
J. Roche, J. Ying, and A. Bax: Accurate Measurement of (3)JHNHa Couplings in Small or Disordered Proteins from WATERGATE-optimized TROSY Spectra, J. Biomol. NMR. 64, 1-7 (2016). (420.pdf, 750495)(420_SI.pdf, 46396)(DOI)(pubmed)
421.
J. Roche, J. Ying, Y. Shen, D.A. Torchia, and A. Bax: ARTSY-J: Convenient and precise measurement of 3JHNHa couplings in mediume-size proteins from TROSY-HSQC spectra, J. Magn. Reson. 268, 73-81 (2016). (421.pdf, 750495)(421_SI.doc, 46396)(DOI)(pubmed)
422.
J.H. Lee, J. Ying, and A. Bax: Nuclear Magnetic Resonance Observation of a-Synuclein Membrane Interaction by Monitoring the Acetylation Reactivity of Its Lysine Side Chains, Biochemistry 55, 4949-4959 (2016). (422.pdf, 2541100)(422_SI.pdf, 81163)(DOI)(pubmed)
423.
J.M. Louis, J.L. Baber, R. Ghirlando, A. Aniana, A. Bax, J. Roche: Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles, PLoS One 11, e0160597 (2016). (423.pdf, 2829095)(423_SI.pdf, 324210)(DOI)(pubmed)
424.
J.W. Werner-Allen, J.F. DuMond, R.L. Levine, and A. Bax: Toxic Dopamine Metabolite DOPAL Forms an Unexpected Dicatechol Pyrrole Adduct with Lysines of a-Synuclein, Angew. Chem. Int. Ed. Engl. 50, 7374-7378 (2016). (424.pdf, 1832157)(424_SI.pdf, 2111112)(DOI)(pubmed)
425.
J.H. Lee, J. Ying, and A. Bax: Quantitative evaluation of positive Phi angle propensity in flexible regions of proteins from three-bond J couplings, Phys Chem Chem Phys 18, 5759-5770 (2016). (425.pdf, 2938897)(425_SI.pdf, 197951)(DOI)(pubmed)
426.
J. Li, Y. Wang, J. Chen, Z. Liu, A. Bax, L. Yao : Observation of a-Helical Hydrogen-Bond Cooperativity in an Intact Protein, J. Am. Chem. Soc. 138, 1824-1827 (2016). (426.pdf, 902231)(426_SI.pdf, 344010)(DOI)(pubmed)
427.
J. Roche, Y. Shen, J.H. Lee, J. Ying, and A. Bax: Monomeric Aß(1-40) and Aß(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil, Biochemistry 55, 762-775 (2016). (427.pdf, 2845746)(427_SI.pdf, 1113166)(DOI)(pubmed)
428.
T.R. Alderson, and A. Bax: Parkinson's disease: Disorder in the court, Nature 530, 38-39 (2016). (428.pdf, 2541100)(DOI)(pubmed)
429.
J. Ying, F. Delaglio, D.A. Torchia, and A. Bax: Sparse Multidimensional Iterative Lineshape-Enhanced (SMILE) Reconstruction of Both Non-Uniformly Sampled and Conventional NMR Data, J. Biomol. NMR. 68, 101-118 (2017). (429.pdf, 1823907)(DOI)(429_SI.pdf, 539888)(pubmed)
430.
M. Perni, C. Galvagnion; A. Maltsev, G. Meisl, M.B.D. Muller; P.K. Chala; J.B. Kirkegaard; P. Flagmeier; S.I.A. Cohen, R. Cascella, S.W. Chen, R. Limboker, P. Sormanni, G.T. Heller, F.A. Aprile, N. Cremades, C. Cecchi, F. Chiti, E.A.A. Nollen, T.P.J. Knowles, M. Vendruscolo, A. Bax, M. Zasloff; C.M. Dobson: A natural product inhibits the initiation of alpha-synuclein aggregation and suppresses its toxicity, Proc. Natl. Acad. Sci. USA 114, E1009-E1017 (2017). (430.pdf, 3085911)(430_SI.pdf, 548532)(DOI)(pubmed)
431.
K. Natarajan, A.C. McShan, J. Jiang, V.K. Kumirov, R. Wang, H. Zhao, P. Schuck, M.E. Tilahun, L.F. Boyd, J. Ying, A. Bax, D.H. Margulies and N.G. Sgourakis: An allosteric site in the T cell receptor ßchain constant domain plays a critical role in T cell signaling. Nature Comm. 8:15260 (2017). (431.pdf, 2359031)(431_SI.pdf, 6169895)(DOI)(pubmed)
432.
J.W. Werner-Allen, R.L. Levine, and A. Bax: Superoxide is the critical driver of DOPAL autoxidation, lysyl adduct formation, and crosslinking of a-synuclein. Biochem. Biophys. Res. Commun. 48:281-286 (2017). (432.pdf, 934224)(432_SI.doc, 402944)(DOI)(pubmed)
433.
E. Stolzenberg, D. Berry, D. Yang, E.Y. Lee, A. Kroemer, S. Kaufman, G.C.L. Wong, J.J. Oppenheim, S. Sen, T. Fishbein, A. Bax, B. Harris, D. Barbut, M.A. Zasloff: A Role for Neuronal Alpha-Synuclein in Gastrointestinal Immunity. J. Innate. Immun. 9, 456-463 (2017). (433.pdf, 397289)(433_SI.docx, 530889)(DOI)(pubmed)
434.
T.R. Alderson, C., Charlier, D.A. Torchia, P. Anfinrud,and A. Bax: Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy. J. Am. Chem. Soc. 139, 11036-11039 (2017) (434.pdf, 807697) (434_SI.pdf, 1912680)(DOI)(pubmed)
435.
Y. Shen, J. Roche, A. Grishaev and A. Bax: Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins. Protein Sci. 27, 146-158 (2018).(435.pdf, 1566287) (435_SI.doc, 2260992)(DOI)(pubmed)
S.C. Chiliveri, J.M. Louis, R. Ghirlando, J.L. Baber, and A. Bax: Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings J. Am. Chem. Soc. 140, 34-37 (2018).(437.pdf, 658001) (437_SI.pdf, 931971)(DOI)(pubmed)
438.
C. Charlier, T.R. Alderson, J.M. Courtney, J. Ying, P. Anfinrud, and A. Bax. Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell. Proc. Natl. Acad. Sci. USA 115, E4169-E4178 (2018).(438.pdf, 1716576) (438_SI.pdf, 1076763)(DOI)(pubmed)(c&en news)(Youtube Video)
439.
J.W. Werner-Allen, S. Monti, J.F. DuMond, R.L. Levine, and A. Bax: Isoindole Linkages Provide a Pathway for DOPAL-Mediated Cross-Linking of a-Synuclein. Biochemistry. 57(9):1462-1474 (2018). (439.pdf, 2831914)(439_SI.pdf, 816292)(DOI)(pubmed)
440.
K. Natarajan, J. Jiang, N.A. May, M.G. Mage, L.F. Boyd, A.C. McShan, N.G. Sgourakis, A. Bax, and D.H. Margulies: The Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling. Front. Immunol. 9:1657 (2018). (440.pdf, 1268424)(DOI)(pubmed)
441.
C. Charlier, J.M. Courtney, P. Anfinrud, and A. Bax: Interrupted Pressure-Jump NMR Experiments Reveal Resonances of On-Pathway Protein Folding Intermediate. J. Phys. Chem. B. 122(49):11792-11799 (2018). (441.pdf, 1830004)(441_SI.pdf, 667263)(DOI)(pubmed)
442.
T.R. Alderson, J. Roche, H.Y. Gastall, D.M. Dias, I. Pritišanac, J. Ying, A. Bax, J.L.P. Benesch, and A.J. Baldwin: Local unfolding of the HSP27 monomer regulates chaperone activity. Nat. Commun. 10(1):1068 (2019). (442.pdf, 3602800)(442_SI.pdf, 3741763)(DOI)(pubmed)
443.
C.A. Barnes, Y. Shen, J. Ying, Y. Takagi, D. A. Torchia, J.R. Sellers, and A. Bax: Remarkable Rigidity of the Single Alpha-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy. J. Am. Chem. Soc. 141, 9004-9017 (2019). (443.pdf, 2330148)(443_SI.pdf, 3741763)(DOI)(pubmed)
444.
J. Ying, C.A. Barnes, J.M. Louis, and A. Bax: Importance of time-ordered non-uniform sampling of multi-dimensional NMR spectra of Aß1–42 peptide under aggregating conditions. J. Biomol. NMR. 73, 429-441 (2019). (444.pdf, 2816251)(444_SI.pdf, 1187004)(DOI)(pubmed)
445.
A. Bax, G.M. Clore: Protein NMR: Boundless opportunities. J. Magn. Reson. 306, 187-191 (2019). (445.pdf, 289519)(DOI)(pubmed)
446.
C.A. Barnes, A.J. Robertson, J.M. Louis, P. Anfinrud, and A. Bax: Observation of ß-Amyloid Peptide Oligomerization by Pressure-Jump NMR Spectroscopy. J. Am. Chem. Soc. 141, 13762-13766 (2019). (446.pdf, 1576682)(446_SI.pdf, 1160343)(DOI)(pubmed)
447.
V. Ramanujam, C. Charlier, and A. Bax: Observation and Kinetic Characterization of Transient Schiff Base Intermediates by CEST NMR Spectroscopy. Angew. Chem. Int. Ed. Engl. 58, 15309-15312 (2019). (447.pdf, 2403127)(447_SI.pdf, 981777)(DOI)(pubmed)
448.
J. Marchant, A. Bax, and M.F. Summers: Accurate Measurement of Residual Dipolar Couplings in Large RNAs by Variable Flip Angle NMR. J. Am. Chem. Soc. 140, 6978-6983 (2018). (448.pdf, 2039808)(448_SI.pdf, 3567616)(DOI)(pubmed)
449.
P. Anfinrud, V. Stadnytskyi, C.E. Bax, and A. Bax: Visualizing Speech-Generated Oral Fluid Droplets with Laser Light Scattering. N. Engl. J. Med. 382, 2061-2063 (2020). (449.pdf, 428091)(DOI)(pubmed)
450.
V. Stadnytskyi, C.E. Bax, A. Bax, and P. Anfinrud: The airborne lifetime of small speech droplets and their potential importance in SARS-CoV-2 transmission. Proc. Natl. Acad. Sci. USA 117, 11875-11877 (2020). (450.pdf, 597435)(DOI)(pubmed)
451.
V. Ramanujam, T.R. Alderson, I. Pritišanac, J. Ying, and A. Bax: Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy. J. Magn. Reson. 312, 106701 (2020). (451.pdf, 1615254)(451_SI.pdf, 678954)(DOI)(pubmed)
T. Kakeshpour, V. Ramanujam, C.A. Barnes, Y. Shen, J. Ying, and A. Bax: A lowly populated, transient ßsheet structure in monomeric Aß1-42 identified by multinuclear NMR of chemical denaturation. Biophys. Chem. 270, 106531 (2021). (456.pdf, 2907452 Bytes)(456_SI.pdf, 1259153 Bytes)(DOI)(pubmed)
A.J. Robertson, J. Ying and A. Bax: Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis. Magn. Reson. 2, 129-138 (2021). (458.pdf, 2473673 Bytes)(458_SI.pdf, 1120987 Bytes)(DOI)(pubmed)
S.C. Chiliveri, J.M. Louis, R. Ghirlando, and A. Bax: Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion. Sci. Adv. 7, eabk2226 (2021).(460.pdf, 3052117 Bytes)(460_SI.pdf, 6222126 Bytes)(DOI)(pubmed)
461.
P. Kushalnagar, C.C. Chow, and A. Bax: Self-infection with speech aerosol may contribute to COVID-19 severity. J. Intern. Med. 290, 1275-1277 (2021).(461.pdf, 306464 Bytes)(DOI)(pubmed)
462.
V. Stadnytskyi, P. Anfinrud, and A. Bax: Breathing, speaking, coughing or sneezing: What drives transmission of SARS-CoV-2? J. Intern. Med. 290, 1010-1027 (2021).(462.pdf, 2337914 Bytes)(DOI)(pubmed)
463.
A.J. Robertson, J.M. Courtney, Y. Shen, J. Ying and A. Bax: Concordance of X-ray and AlphaFold2 Models of SARS-CoV-2 Main Protease with Residual Dipolar Couplings Measured in Solution. J. Am. Chem. Soc. 143, 19306-19310 (2021).(463.pdf, 2,171,688 Bytes)(463_SI.pdf, 4,673,963 Bytes)(DOI)(pubmed)
S.C. Chiliveri, A.J. Robertson, Y. Shen,, D.A. Torchia, and A. Bax: Advances in NMR Spectroscopy of Weakly Aligned Biomolecular Systems. Chem. Rev. (2021).(465.pdf, 3,791,459 Bytes)(DOI)(pubmed)
466.
T. Kakeshpour, B. Metaferia, R.N. Zare, and A. Bax: Quantitative detection of hydrogen peroxide in rain, air, exhaled breath, and biological fluids by NMR spectroscopy. Proc. Natl. Acad. Sci. USA 119, e2121542119 (2022).(466.pdf, 803,558 Bytes)(DOI)(pubmed)
Y. Shen, J.M. Courtney, P. Anfinrud, and A. Bax: Hybrid measurement of respiratory aerosol reveals a dominant coarse fraction resulting from speech that remains airborne for minutes. Proc. Natl. Acad. Sci. USA 119(26), e2203086119 (2022).(468.pdf, 2,128,518)(468_SI.pdf, 217,475)(DOI)(pubmed)
469.
S.C. Chiliveri, J.M. Louis, R.B. Best, and A. Bax: Real-time Exchange of the Lipid-bound Intermediate and Post-fusion States of the HIV-1 gp41 Ectodomain. J. Mol. Biol. 434, 167683 (2022).(469.pdf, 1,618,088)(469_SI.pdf, 4,049,740)(DOI)(pubmed)
470.
A. Robertson, J. Ying, and A. Bax: NMR Observation of Sulfhydryl Signals in SARS-CoV-2 Main Protease Aids Structural Studies. Chembiochem. 23(19), e202200471 (2022).(470.pdf, 996,266)(470_SI.pdf, 8,002,515)(DOI)(pubmed)
471.
A. Bax, Y. Shen, T. Kakeshpour, K.P. Fennelly: Snoring may transmit infectious aerosols from the upper to the lower respiratory tract. Med. Hypotheses. 168, 110966 (2022).(471.pdf, 848,479)(DOI)(pubmed)
472.
A. Ceccon A, V. Tugarinov, A. Bax, G.M. Clore: Global Dynamics and Exchange Kinetics of a Protein on the Surface of Nanoparticles Revealed by Relaxation-Based Solution NMR Spectroscopy. J. Am. Chem. Soc. 138(18), 5789-92(2016).(472.pdf, 1,882,619)(472_SI.pdf, 1,754,145)(DOI)(pubmed)
