Fast NMR method to probe solvent accessibility and disordered regions in proteins.

ABSTRACT: Understanding protein structure and dynamics, which govern key cellular processes, is crucial for basic and applied research. Intrinsically disordered protein (IDP) regions display multifunctionality via alternative transient conformations, being key players in disease mechanisms. IDP regions are abundant, namely in small viruses, allowing a large number of functions out of a small proteome. The relation between protein function and structure is thus now seen from a different perspective: as IDP regions enable transient structural arrangements, each conformer can play different roles within the cell. However, as IDP regions are hard and time-consuming to study via classical techniques (optimized for globular proteins with unique conformations), new methods are required. Here, employing the

SUBMITTER: Faustino AF 

PROVIDER: S-EPMC6367444 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature