Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling.

ABSTRACT: Chaperones maintain a healthy proteome by preventing aggregation and by aiding in protein folding. Precisely how chaperones influence the conformational properties of their substrates, however, remains unclear. To achieve a detailed description of dynamic chaperone-substrate interactions, we fused site-specific NMR information with coarse-grained simulations. Our model system is the binding and folding of a chaperone substrate, immunity protein 7 (Im7), with the chaperone Spy. We first used an automated procedure in which NMR chemical shifts inform the construction of system-specific force fields that describe each partner individually. The models of the two binding partners are then combined to perform simulations on the chaperone-substrate complex. The binding simulations show excellent

SUBMITTER: Salmon L 

PROVIDER: S-EPMC5242313 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature