Funneled energy landscape unifies principles of protein binding and evolution.

ABSTRACT: Most proteins have evolved to spontaneously fold into native structure and specifically bind with their partners for the purpose of fulfilling biological functions. According to Darwin, protein sequences evolve through random mutations, and only the fittest survives. The understanding of how the evolutionary selection sculpts the interaction patterns for both biomolecular folding and binding is still challenging. In this study, we incorporated the constraint of functional binding into the selection fitness based on the principle of minimal frustration for the underlying biomolecular interactions. Thermodynamic stability and kinetic accessibility were derived and quantified from a global funneled energy landscape that satisfies the requirements of both the folding into the stable structure

SUBMITTER: Yan Z 

PROVIDER: S-EPMC7959555 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature