期刊
PROTEIN SCIENCE
卷 20, 期 5, 页码 773-782出版社
WILEY-BLACKWELL
DOI: 10.1002/pro.614
关键词
NMR; protein function; protein regulation; allosteric interactions; autoinhibition
资金
- NIHGMS [GM073854, GM080308]
- NSF MCB [0618259, 0842491]
- Protein Society
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0618259, 1121896] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0842491] Funding Source: National Science Foundation
NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site-resolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.
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