Influence of mutation bias and hydrophobicity on the substitution rates and sequence entropies of protein evolution.

ABSTRACT: The number of amino acids that occupy a given protein site during evolution reflects the selective constraints operating on the site. This evolutionary variability is strongly influenced by the structural properties of the site in the native structure, and it is quantified either through sequence entropy or through substitution rates. However, while the sequence entropy only depends on the equilibrium frequencies of the amino acids, the substitution rate also depends on the exchangeability matrix that describes mutations in the mathematical model of the substitution process. Here we apply two variants of a mathematical model of protein evolution with selection for protein stability, both against unfolding and against misfolding. Exploiting the approximation of independent sites, these mode

SUBMITTER: Jimenez-Santos MJ 

PROVIDER: S-EPMC6174885 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature