Dr. Markus Zweckstetter

National Institutes of Health
Building 5, Room B1-28
9000 Rockville Pike
Bethesda, MD 20892-0520

Tel.: 301-496-7902
Fax: 301-496-0825

E-mail: zweckste@speck.niddk.nih.gov


Structure determination of macromolecules & NMR methods


Ph.D, 1998, Structural Biology (`magna cum laude`)
Max Planck Institute for Biochemistry, Germany

`Diplom` (M.S.), 1996, Physics (`with distinction`)
Ludwig Maximilians University Munich, Germany


Post-Doctoral Fellow
National Institutes of Health, Bethesda, Maryland, USA , 1999-present

Post-Doctoral Fellow
Max Planck Institute for Biochemistry, Department Structure Research, 1998-1999

Network Administrator and operator of a 600 MHz NMR spectrometer
Max Planck Institute for Biochemistry, Department Structure Research, 1996-1999


Emmy Noether-programme of the Deutsche Forschungsgemeinschaft, 1999 - present
Student travel stipend recipient, 40th ENC, Orlando, Florida, USA, 1999
Ph.D grant recipient, fellowship of the 'Verbandes der Chemischen Industrie', 1996-1998
Passed with distinction ('Diplom' in physics), Ludwig Maximilians University Munich, Germany, 1996
Grant recipient, scholarship of the German Academic Exchange Service (DAAD), 1993-1994


Publications from the Bax Group
Previous  Publications:

Zweckstetter, M. & Holak, T. A. (1999). Robust refocusing of 13C-magnetization in multidimensional NMR experiments by adiabatic fast passage pulses. J. Biomol. NMR., 15, 331-334.

Pfänder, R., Neumann, L., Zweckstetter, M., Seger, C., Holak, T. A. & Tampe, R. (1999). Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. Biochemistry 38, 13692-13698.

Zweckstetter, M. & Holak, T. A. (1998). An adiabatic multiple spin-echo pulse sequence: removal of systematic errors due to pulse imperfections and off-revesonance effects. J. Magn. Reson. 133, 134-147.

Kalus, W., Zweckstetter, M., Renner, C., Sanchez, Y., Georgescu, J., Grol, M., Demuth, D., Schumacher, R., Dony, C., Lang, K. & Holak, T. A. (1998). Structure of the IGF binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions. EMBO J. 17, 6558-6572.

Mühlhahn, P., Zweckstetter, M., Georgescu, J., Ciosto, C., Renner, C., Lanzendörfer, M., Lang, K., Ambrosius, D., Baier, M., Kurth, R. & Holak, T. A. (1998). Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site. Nat. Struct. Biol. 8, 682-686.

Kohfeldt, E., Göhring, W., Mayer, U., Zweckstetter, M., Mayer, U., Holak, T. A., Chu, M.-L. & Timpl, R. (1996). Conversion of the Kunitz-type module of collagen VI into a highly active trypsin inhibitor by site-directed mutagenesis. Eur. J. Biochem. 238, 333-340.

Zweckstetter, M., Czisch, M., Mayer, U., Chu, M.-L., Zinth, W., Timpl, R. & Holak, T. A. (1996). Structure and multiple conformations of the Kunitz-type domain from human type VI collagen alpha 3(VI) chain in solution. Structure 4, 195-209.



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