Evidence for the principle of minimal frustration in the evolution of protein folding landscapes.

ABSTRACT: Theoretical and experimental studies have firmly established that protein folding can be described by a funneled energy landscape. This funneled energy landscape is the result of foldable protein sequences evolving following the principle of minimal frustration, which allows proteins to rapidly fold to their native biologically functional conformations. For a protein family with a given functional fold, the principle of minimal frustration suggests that, independent of sequence, all proteins within this family should fold with similar rates. However, depending on the optimal living temperature of the organism, proteins also need to modulate their thermodynamic stability. Consequently, the difference in thermodynamic stability should be primarily caused by differences in the unfolding rates

SUBMITTER: Tzul FO 

PROVIDER: S-EPMC5338549 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature