Inferring repeat-protein energetics from evolutionary information.

ABSTRACT: Natural protein sequences contain a record of their history. A common constraint in a given protein family is the ability to fold to specific structures, and it has been shown possible to infer the main native ensemble by analyzing covariations in extant sequences. Still, many natural proteins that fold into the same structural topology show different stabilization energies, and these are often related to their physiological behavior. We propose a description for the energetic variation given by sequence modifications in repeat proteins, systems for which the overall problem is simplified by their inherent symmetry. We explicitly account for single amino acid and pair-wise interactions and treat higher order correlations with a single term. We show that the resulting evolutionary field can

SUBMITTER: Espada R 

PROVIDER: S-EPMC5491312 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature