Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.

ABSTRACT: Proteins that lack tertiary stability under normal conditions, known as intrinsically disordered, exhibit a wide range of biological activities. Molecular descriptions for the biology of intrinsically disordered proteins (IDPs) consequently rely on disordered structural models, which in turn require experiments that assess the origins to structural features observed. For example, while hydrodynamic size is mostly insensitive to sequence composition in chemically denatured proteins, IDPs show strong sequence-specific effects in the hydrodynamic radius (R_h ) when measured under normal conditions. To investigate sequence-modulation of IDP R_h , disordered ensembles generated by a hard sphere collision model modified with a structure-based parameterization of the solution

SUBMITTER: English LR 

PROVIDER: S-EPMC5258847 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature