Protein unfolding rates correlate as strongly as folding rates with native structure.

ABSTRACT: Although the folding rates of proteins have been studied extensively, both experimentally and theoretically, and many native state topological parameters have been proposed to correlate with or predict these rates, unfolding rates have received much less attention. Moreover, unfolding rates have generally been thought either to not relate to native topology in the same manner as folding rates, perhaps depending on different topological parameters, or to be more difficult to predict. Using a dataset of 108 proteins including two-state and multistate folders, we find that both unfolding and folding rates correlate strongly, and comparably well, with well-established measures of native topology, the absolute contact order and the long range order, with correlation coefficient values of 0.75 o

SUBMITTER: Broom A 

PROVIDER: S-EPMC4380988 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature