The relationship between relative solvent accessibility and evolutionary rate in protein evolution.

ABSTRACT: Recent work with Saccharomyces cerevisiae shows a linear relationship between the evolutionary rate of sites and the relative solvent accessibility (RSA) of the corresponding residues in the folded protein. Here, we aim to develop a mathematical model that can reproduce this linear relationship. We first demonstrate that two models that both seem reasonable choices (a simple model in which selection strength correlates with RSA and a more complex model based on RSA-dependent amino acid distributions) fail to reproduce the observed relationship. We then develop a model on the basis of observed site-specific amino acid distributions and show that this model behaves appropriately. We conclude that evolutionary rates are directly linked to the distribution of amino acids at individual sites. B

SUBMITTER: Ramsey DC 

PROVIDER: S-EPMC3122320 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature