Capturing conformational States in proteins using sparse paramagnetic NMR data.

ABSTRACT: Capturing conformational changes in proteins or protein-protein complexes is a challenge for both experimentalists and computational biologists. Solution nuclear magnetic resonance (NMR) is unique in that it permits structural studies of proteins under greatly varying conditions, and thus allows us to monitor induced structural changes. Paramagnetic effects are increasingly used to study protein structures as they give ready access to rich structural information of orientation and long-range distance restraints from the NMR signals of backbone amides, and reliable methods have become available to tag proteins with paramagnetic metal ions site-specifically and at multiple sites. In this study, we show how sparse pseudocontact shift (PCS) data can be used to computationally model conformatio

SUBMITTER: Pilla KB 

PROVIDER: S-EPMC4436263 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature