Characterization of protein folding by a Φ-value calculation with a statistical-mechanical model.

ABSTRACT: The Φ-value analysis approach provides information about transition-state structures along the folding pathway of a protein by measuring the effects of an amino acid mutation on folding kinetics. Here we compared the theoretically calculated Φ values of 27 proteins with their experimentally observed Φ values; the theoretical values were calculated using a simple statistical-mechanical model of protein folding. The theoretically calculated Φ values reflected the corresponding experimentally observed Φ values with reasonable accuracy for many of the proteins, but not for all. The correlation between the theoretically calculated and experimentally observed Φ values strongly depends on whether the protein-folding mechanism assumed in the model holds true in real proteins. In other words, the c

SUBMITTER: Wako H 

PROVIDER: S-EPMC5221509 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature