NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.

ABSTRACT: In order to understand the conformational behavior of intrinsically disordered proteins (IDPs) and their biological interaction networks, the detection of residual structure and long-range interactions is required. However, the large number of degrees of conformational freedom of disordered proteins require the integration of extensive sets of experimental data, which are difficult to obtain. Here, we provide a straightforward approach for the detection of residual structure and long-range interactions in IDPs under near-native conditions using solvent paramagnetic relaxation enhancement (sPRE). Our data indicate that for the general case of an unfolded chain, with a local flexibility described by the overwhelming majority of available combinations, sPREs of non-exchangeable protons can be

SUBMITTER: Hartlmuller C 

PROVIDER: S-EPMC6692294 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature