A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization.

ABSTRACT: We have determined the effect of mutations involving isoleucine and valine (i.e., mutations I-->V and V-->I) on the stability of Escherichia coli thioredoxin. Despite the similarity in chemical structure (V and I differ only in a methyl group), we find that many environments are optimized to a significant extent for either V or I. We find, furthermore, that a plot of effect of hydrophobic mutations on stability versus packing density shows a strikingly simple pattern that clearly reflects evolutionary structural optimization. The existence of such patterns suggests the possibility of rationalizing (and perhaps even predicting) mutation effects on protein stability on the basis of evolutionary models. By "evolutionary model" we specifically refer in this context to a model for mutation effe

SUBMITTER: Godoy-Ruiz R 

PROVIDER: S-EPMC1366828 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature