Toward Accurate Coarse-Grained Simulations of Disordered Proteins and Their Dynamic Interactions.

ABSTRACT: Intrinsically disordered proteins (IDPs) play crucial roles in cellular regulatory networks and are now recognized to often remain highly dynamic even in specific interactions and assemblies. Accurate description of these dynamic interactions is extremely challenging using atomistic simulations because of the prohibitive computational cost. Efficient coarse-grained approaches could offer an effective solution to overcome this bottleneck if they could provide an accurate description of key local and global properties of IDPs in both unbound and bound states. The recently developed hybrid-resolution (HyRes) protein model has been shown to be capable of providing a semiquantitative description of the secondary structure propensities of IDPs. Here, we show that greatly improved description of

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC9910785 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature