Mutational effects on stability are largely conserved during protein evolution.

ABSTRACT: Protein stability and folding are the result of cooperative interactions among many residues, yet phylogenetic approaches assume that sites are independent. This discrepancy has engendered concerns about large evolutionary shifts in mutational effects that might confound phylogenetic approaches. Here we experimentally investigate this issue by introducing the same mutations into a set of diverged homologs of the influenza nucleoprotein and measuring the effects on stability. We find that mutational effects on stability are largely conserved across the homologs. We reach qualitatively similar conclusions when we simulate protein evolution with molecular-mechanics force fields. Our results do not mean that proteins evolve without epistasis, which can still arise even when mutational stabilit

SUBMITTER: Ashenberg O 

PROVIDER: S-EPMC3876214 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature