Diversity of hydrodynamic radii of intrinsically disordered proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) form an important class of biomolecules regulating biological processes in higher organisms. The lack of a fixed spatial structure facilitates them to perform their regulatory functions and allows the efficiency of biochemical reactions to be controlled by temperature and the cellular environment. From the biophysical point of view, IDPs are biopolymers with a broad configuration state space and their actual conformation depends on non-covalent interactions of its amino acid side chain groups at given temperature and chemical conditions. Thus, the hydrodynamic radius (R_h) of an IDP of a given polymer length (N) is a sequence- and environment-dependent variable. We have reviewed the literature values of hydrodynamic radii of IDPs determine

SUBMITTER: Bialobrzewski MK 

PROVIDER: S-EPMC10618399 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature