Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions.

ABSTRACT: Being responsible for more than 90% of cellular functions, protein molecules are workhorses in all the life forms. In order to cater for such a high demand, proteins have evolved to adopt diverse structures that allow them to perform myriad of functions. Beginning with the genetically directed amino acid sequence, the classical understanding of protein function involves adoption of hierarchically complex yet ordered structures. However, advances made over the last two decades have revealed that inasmuch as 50% of eukaryotic proteome exists as partially or fully disordered structures. Significance of such intrinsically disordered proteins (IDPs) is further realized from their ability to exhibit multifunctionality, a feature attributable to their conformational plasticity. Among the coded am

SUBMITTER: Bhopatkar AA 

PROVIDER: S-EPMC8048112 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature