Protein folding, protein collapse, and tanford's transfer model: lessons from single-molecule FRET.

ABSTRACT: The essential and nontrivial role of the denatured state of proteins in their folding reaction is being increasingly scrutinized in recent years. Single molecule FRET (smFRET) experiments show that the denatured state undergoes a continuous collapse (or coil-to-globule) transition as the concentration of a chemical denaturant is decreased, suggesting that conformational entropy of the denatured state is an important part of the free energy of folding. Such observations question the validity of the classical Tanford transfer model, which suggests that the folding free energy can be understood solely based on the difference in amino acid solvation between the folded state and a fixed unfolded state. An alternative to the transfer model is obtained here from a polymer theoretical analysis of

SUBMITTER: Ziv G 

PROVIDER: S-EPMC2663972 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature