Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.

ABSTRACT: Experimental studies have shown that some proteins exist in two alternative native-state conformations. It has been proposed that such bi-stable proteins can potentially function as evolutionary bridges at the interface between two neutral networks of protein sequences that fold uniquely into the two different native conformations. Under adaptive conflict scenarios, bi-stable proteins may be of particular advantage if they simultaneously provide two beneficial biological functions. However, computational models that simulate protein structure evolution do not yet recognize the importance of bi-stability. Here we use a biophysical model to analyze sequence space to identify bi-stable or multi-stable proteins with two or more equally stable native-state structures. The inclusion of such prot

SUBMITTER: Sikosek T 

PROVIDER: S-EPMC3441461 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature