U.S. Department of Health and Human Services
Hoi Sung Chung

 Contact Info

Tel: 301-496-0202
Email: chunghoi@niddk.nih.gov

 Select Experience

  • Ph.D.Massachusetts Institute of Technology2007
  • M.S.Seoul National University2000
  • B.S.Seoul National University1998

 Related Links


Hoi Sung Chung, Ph.D.

Investigator, Biophysical Chemistry SectionLaboratory of Chemical Physics
  • Biomedical Engineering/Biophysics/Physics
  • Structural Biology
Research Summary/In Plain Language

Research in Plain Language

Proteins play critical roles in virtually every cellular process. To perform their biological functions, they must properly fold into a unique three-dimensional structure. However, it is predicted that a surprisingly large fraction (> 30 percent) of proteins stay unfolded or contain unstructured regions. These unstructured proteins are called intrinsically disordered proteins (IDPs). Interestingly, IDPs fold when performing their biological functions: binding to target proteins. The intrinsic disorder is found in many proteins performing central roles in cellular regulation such as gene transcription and signal transduction and therefore is frequently implicated in the development of various diseases such as cancers. In addition, disordered proteins are often prone to aggregation, which also causes various protein misfolding diseases such as Alzheimer’s disease and Parkinson’s disease.

We study protein binding and aggregation processes of IDPs by watching one molecule at a time using single molecule spectroscopy. Recent development of various single molecule techniques has allowed monitoring heterogeneous biological processes. Studying the heterogeneity is particularly important for understanding the binding and aggregation mechanisms because conformational transitions of proteins are intrinsically heterogeneous.