Dataset Information


Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation.

ABSTRACT: Protein function depends critically on intrinsic internal dynamics, which is manifested in distinct ways, such as loop motions that regulate protein recognition and catalysis. Under physiological conditions, dynamic processes occur on a wide range of time scales from subpicoseconds to seconds. Commonly used NMR spin relaxation in solution provides valuable information on very fast and slow motions but is insensitive to the intermediate nanosecond to microsecond range that exceeds the protein tumbling correlation time. Presently, very little is known about the nature and functional role of these motions. It is demonstrated here how transverse spin relaxation becomes exquisitely sensitive to these motions at atomic resolution when studying proteins in the presence of nanoparticles. Application of this novel cross-disciplinary approach reveals large-scale dynamics of loops involved in functionally critical protein-protein interactions and protein-calcium ion recognition that were previously unobservable.

PROVIDER: S-EPMC6693908 | BioStudies |

REPOSITORIES: biostudies

Similar Datasets

| S-EPMC5953972 | BioStudies
| S-EPMC8018934 | BioStudies
| S-EPMC2553144 | BioStudies
| S-EPMC2864776 | BioStudies
2016-01-01 | S-EPMC5010779 | BioStudies
| S-EPMC3676944 | BioStudies
| S-EPMC4190660 | BioStudies
| S-EPMC3985601 | BioStudies
| S-EPMC3865798 | BioStudies
| S-EPMC2553108 | BioStudies