Cytochrome c Folding

*********************************************************************

How a protein folds into its three dimensional structure is one of the central questions in molecular biology and in the biotechnology industry. To advance the understanding of protein folding, it is necessary to determine the structures and the kinetics of the intermediates in the folding pathway. For this, we developed submillisecond mixers in which folding can be initiated in less than 100 microseconds, a time scale that is over an order of magnitude faster than previously possible. This has allowed us to discover a new model that accounts for the folding of cytochrome c from 100 microseconds to the formation of the native state. Many new experiments with several different techniques, icluding reasonance Raman scattering, fluorescence quenching measurements of tryptophan and CD, will be done to test the generality of this model and its possible role in other proteins.

Horse Heart Cytochrome c Kinetic Model for the Folding Reaction

--- Click here to Check out the related Publications: Cyt c ---

--- Click here to Check out PDB Entry: 1HRC ---

--- Link to Other Protein Folding Groups: Protein Folders ---

--- Link to Chaperonin Home Page: Chaperonin ---

*********************************************************************

Syun-Ru Yeh's Page | Denis Rousseau's Page

Albert Einstein College of Medicine | Department of Physiology and Biophysics