Hoi Sung Chung, Ph.D.
Single-Molecule Biophysics Section, Laboratory of Chemical Physics
Building 5, Room 124
5 Memorial Dr
Bethesda, MD 20814
+1 301 496 0202
Single Protein Conformational Dynamics: Folding, Binding, and Aggregation of Disordered Proteins
We study conformational dynamics of proteins using single molecule Förster resonance energy transfer (FRET) spectroscopy. Especially, we focus on intrinsically disordered proteins (IDPs) that are closely related to various human diseases. The primary goal of our research is to understand the mechanisms of binding and aggregation processes of IDPs.
- Understanding binding mechanism of IDPs. We try to understand the mechanistic details of binding: how molecular conformations evolve when two molecules approach to each other, make a contact, and form a bound complex. This information is contained in the moment of binding that can be probed only by single molecule spectroscopy.
- Characterization of the early stage of aggregation. Protein or peptide oligomers are thought to be implicated in the development of various neurodegenerative diseases. However, oligomerization has been extremely difficult to study due to the heterogeneity of the process. Single molecule spectroscopy can effectively characterize this complicated process by detecting individual oligomers without separation.
Postdoctoral positions are available. To apply email a CV, bibliography, brief summary of research accomplishments, and the names of references.
My group is located at the NIH main campus:
Please visit my group's website for more information
- Ph.D., Massachusetts Institute of Technology, 2007
- M.S., Seoul National University, 2000
- B.S., Seoul National University, 1998
Kim JY, Chung HS. Disordered proteins follow diverse transition paths as they fold and bind to a partner. Science. 2020;368(6496):1253-1257.
Yoo J, Kim JY, Louis JM, Gopich IV, Chung HS. Fast three-color single-molecule FRET using statistical inference. Nat Commun. 2020;11(1):3336.
Kim JY, Meng F, Yoo J, Chung HS. Diffusion-limited association of disordered protein by non-native electrostatic interactions. Nat Commun. 2018;9(1):4707.
Meng F, Bellaiche MMJ, Kim JY, Zerze GH, Best RB, Chung HS. Highly Disordered Amyloid-β Monomer Probed by Single-Molecule FRET and MD Simulation. Biophys J. 2018;114(4):870-884.
Chung HS, Meng F, Kim JY, McHale K, Gopich IV, Louis JM. Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET. Proc Natl Acad Sci U S A. 2017;114(33):E6812-E6821.
Related Scientific Focus Areas
Biomedical Engineering and Biophysics
This page was last updated on October 15th, 2020