Evolution of structurally disordered proteins promotes neostructuralization.

ABSTRACT: Protein structure is generally more conserved than sequence, but for regions that can adopt different structures in different environments, does this hold true? Understanding how structurally disordered regions evolve altered secondary structure element propensities as well as conformational flexibility among paralogs are fundamental questions for our understanding of protein structural evolution. We have investigated the evolutionary dynamics of structural disorder in protein families containing both orthologs and paralogs using phylogenetic tree reconstruction, protein structure disorder prediction, and secondary structure prediction in order to shed light upon these questions. Our results indicate that the extent and location of structurally disordered regions are not universally conser

SUBMITTER: Siltberg-Liberles J 

PROVIDER: S-EPMC3108607 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature