Quantitative prediction of ensemble dynamics, shapes and contact propensities of intrinsically disordered proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) are highly dynamic systems that play an important role in cell signaling processes and their misfunction often causes human disease. Proper understanding of IDP function not only requires the realistic characterization of their three-dimensional conformational ensembles at atomic-level resolution but also of the time scales of interconversion between their conformational substates. Large sets of experimental data are often used in combination with molecular modeling to restrain or bias models to improve agreement with experiment. It is shown here for the N-terminal transactivation domain of p53 (p53TAD) and Pup, which are two IDPs that fold upon binding to their targets, how the latest advancements in molecular dynamics (MD) simulations methodology

SUBMITTER: Yu L 

PROVIDER: S-EPMC9491582 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature