hoisunglab
Laboratory of Chemical Physics
NIDDK
NIH
Publications
(44)  E. Lerner, A. Barth, J. Hendrix, B. Ambrose, V. Birkedal, S. C. Blanchard, R. Börner, H. S. Chung, T. Cordes, T. D. Craggs,
       A. A. Deniz, J. Diao, J. Fei, R. L. Gonzalez, Jr., I. V. Gopich, T. Ha, C. A. Hanke, G Haran, N. S. Hatzakis, S. Hohng,
       S.-C. Hong, T. Hugel, A. Ingargiola, C. Joo, A. N. Kapanidis, H. D. Kim, S. H. Kim, T. Laurence, N. K. Lee, T.-H. Lee,
       E. A. Lemke, E. Margeat, J. Michaelis, X. Michalet, S. Myong, D. Nettels, T.-O. Peulen, Y. Razvag, N. C. Robb, B. Schuler,
       H. Soleimaninejad, C. Tang, R. Vafabakhsh, D. C. Lamb, C. A. M. Seidel, S. Weiss, “FRET-based dynamic structural biology:
       challenges, perspectives and an appeal for open-science practices,” eLife 1 20 (2021). [Link]
 
(43)  F. Meng and H. S. Chung, “Kinetics of amyloid beta from deep learning,” News & Views, Nat Comput Sci 1 20 (2021). [Link]
 
(42)  F. Meng*, J. Yoo*, and H. S. Chung, “Heterogeneous aggregation of amyloid-beta 42 from single-molecule spectroscopy,”
       bioRxiv, doi: 10.1101/2020.09.10.290023. (*equally contributed) [Link]
 
(41)  J. -Y. Kim and H. S. Chung, “Disordered proteins follow diverse transition paths as they fold and bind to a partner,” Science 
       368 1253 (2020). [Link]
 
(40)  J. Yoo*, J. -Y. Kim*, J. M. Louis, I. V. Gopich, and H. S. Chung, “Fast three-color single-molecule FRET using statistical
        inference,” Nat Commun 11 3336 (2020). (*equally contributed) [Link]
 
(39)  I. V. Gopich and H. S. Chung, “Theory and Analysis of Single-Molecule FRET Experiments,” in Protein Folding: Theory, 
       Experiments and Simulations, Methods in Molecular Biology, In press.
 
(38)  J. Yoo, J. M. Louis, and H. S. Chung, “Diverse folding pathways of HIV-1 protease monomer on a rugged energy 
       landscape,” Biophys J 117 1456 (2019). [Link]
 
(37)  W. Zheng and H. S. Chung, “Chapter 4: Single-molecule fluorescence studies of IDPs and IDRs,” in Intrinsically disordered
       proteins: Dynamics, binding, and function, edited by N. Salvi, Elsevier, London, 2019. [Link]
 
(36)  M. A. Wälti, J. Steiner, F. Meng, H. S. Chung, J. M. Louis, R. Ghirlando, V. Tugarinov, A. Nath, and G. M. Clore, “Probing the
       mechanism of inhibition of amyloid-b(1-42)-induced neurotoxicity by the chaperonin GroEL,” Proc Natl Acad Sci USA 115 11924
       (2018). [Link]
 
(35)  J. Yoo, J. M. Louis, I. V. Gopich, and H. S. Chung, “Three-color single-molecule FRET and fluorescence lifetime analysis of fast
       protein folding,” J Phys Chem B 122 11702 (2018). [Link]
 
(34)  J. -Y. Kim, F. Meng, J. Yoo, and H. S. Chung, “Diffusion-limited association of disordered protein by non-native electrostatic
       interactions,” Nat Commun 9 4707 (2018). [Link]

(33)  H. S. Chung and W. A. Eaton, “Protein folding transition path times from single molecule FRET,” Curr Opin Struct Biol 48 30 
       (2018). [Link]

(32)  F. Meng*, M. Bellaiche*, J. -Y. Kim, G. Zerze, R. B. Best, and H. S. Chung, “Disordered amyloid b protein
       probed by single molecule FRET and MD simulation,” Biophys J, 114 870 (2018). (*equally contributed) [Link]
 
(31)  H. S. Chung, “Transition path times measured by single-molecule spectroscopy,” J Mol Biol 430 409 (2018). [Link]

(30)  H. S. Chung, F. Meng, J.-Y. Kim, K. McHale, I. V. Gopich, and J. M. Louis, “Oligomerization of the tetramerization domain of
        p53 probed by two- and three-color single-molecule FRET,” Proc Natl Acad Sci USA 114 E6812 (2017). [Link]
 
(29)  H. S. Chung, J. M. Louis, and I. V. Gopich, “Analysis of fluorescence lifetime and energy transfer efficiency in single-molecule
       photon trajectories of fast-folding proteins,” J Phys Chem B 120 680 (2016). [Link]
Publications (- 2015)