A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.

ABSTRACT: Intrinsic flexibility is closely related to protein function, and a plethora of important regulatory proteins have been found to be flexible, multi-domain or even intrinsically disordered. On the one hand, understanding such systems depends on how these proteins behave in solution. On the other, small-angle X-ray scattering (SAXS) is a technique that fulfills the requirements to study protein structure and dynamics relatively quickly with few experimental limitations. Molecular chaperones from Hsp70 and Hsp90 families are multi-domain proteins containing flexible and/or disordered regions that play central roles in cellular proteostasis. Here, we review the structure and function of these proteins by SAXS. Our general approach includes the use of SAXS data to determine size and shape param

SUBMITTER: Borges JC 

PROVIDER: S-EPMC5425780 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature