Hidden folding intermediates in small proteins: Implications for the folding energy landscape, cooperativity, and evolution of protein structures

BIOT 16

Yawen Bai, yawen@helix.nih.gov, Laboratory of Biochemistry and Molecular Biology, NCI,NIH, 37 Convent Drive, Building 37, Room 6114E, Bethesda, MD 20892
Using native-state hydrogen exchange and kinetic methods, we have demonstrated that partially unfolded intermediates can exist after the rate-limiting step in the folding of small proteins and become undetectable in the conventional kinetic folding experiments. Moreover, using a native-state hydrogen exchange-guided protein engineering approach, we have populated such hidden intermediates and solved their high resolution structures by multi-dimensional NMR method. These results and their implications on the folding energy landscape, cooperativity, and structure evolution of proteins will be presented.
 

Biophysical and Biomolecular Symposium: Protein Folding & Characterization
8:00 AM-11:10 AM, Sunday, August 19, 2007 BCEC -- 106, Oral

Division of Biochemical Technology

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007