Hoi Sung Chung, Ph.D.

Investigator

Biophysical Chemistry Section, Laboratory of Chemical Physics

NIDDK

BG 5 RM 101
5 MEMORIAL DR
BETHESDA MD 20814

301-496-0202

chunghoi@niddk.nih.gov

Research Topics

Current Research

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.

  1. 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.
  2. 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.

Fast single-molecule FRET spectroscopy: theory and experiment

Postdoctoral Positions

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.

Biography

  • Ph.D., Massachusetts Institute of Technology, 2007
  • M.S., Seoul National University, 2000
  • B.S., Seoul National University, 1998

Selected Publications

  1. Chung HS. Transition Path Times Measured by Single-Molecule Spectroscopy. J Mol Biol. 2017.

  2. 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.

  3. Chung HS, Louis JM, Gopich IV. Analysis of Fluorescence Lifetime and Energy Transfer Efficiency in Single-Molecule Photon Trajectories of Fast-Folding Proteins. J Phys Chem B. 2016;120(4):680-99.


This page was last updated on April 26th, 2016