Structure of an Intrinsically Disordered Stress Protein Alone and Bound to a Membrane Surface.

ABSTRACT: Dehydrins are a group of intrinsically disordered proteins that protect plants from damage caused by drought, cold, and high salinity. Like other intrinsically disordered proteins, dehydrins can gain structure when bound to a ligand. Previous studies have shown that dehydrins are able to protect liposomes from cold damage, but the interactions that drive membrane binding and the detailed structure of the bound and unbound forms are not known. We use an ensemble-structure approach to generate models of a dehydrin known as K2 in the presence and absence of sodium dodecyl sulfate micelles, and we docked the bound structure to the micelle. The collection of residual dipolar coupling data, amide protection factors, and paramagnetic relaxation enhancement distances, in combination with chemical

SUBMITTER: Atkinson J 

PROVIDER: S-EPMC4982940 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature