Folding of the four-helix bundle FF domain from a compact on-pathway intermediate state is governed predominantly by water motion.

ABSTRACT: Friction plays a critical role in protein folding. Frictional forces originating from random solvent and protein fluctuations both retard motion along the folding pathway and activate protein molecules to cross free energy barriers. Studies of friction thus may provide insights into the driving forces underlying protein conformational dynamics. However, the molecular origin of friction in protein folding remains poorly understood because, with the exception of the native conformer, there generally is little detailed structural information on the other states participating in the folding process. Here, we study the folding of the four-helix bundle FF domain that proceeds via a transiently formed, sparsely populated compact on-pathway folding intermediate whose structure was elucidated previ

SUBMITTER: Sekhar A 

PROVIDER: S-EPMC3511121 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature