Ontology highlight
ABSTRACT:
SUBMITTER: Qin S
PROVIDER: S-EPMC3846091 | biostudies-literature | 2013 Oct
REPOSITORIES: biostudies-literature
The journal of physical chemistry letters 20131001 20
Due to their conformational malleability, intrinsically disordered proteins (IDPs) are particularly susceptible to influences of crowded cellular environments. Here we report a computational study of the effects of macromolecular crowding on the conformational ensemble of a coarse-grained IDP model, by using two approaches. In one, the IDP is simulated along with the crowders; in the other, crowder-free simulations are postprocessed to predict the conformational ensembles under crowding. We foun ...[more]