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NMR reveals novel mechanisms of protein activity regulation

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

  1. NIHGMS [GM073854, GM080308]
  2. NSF MCB [0618259, 0842491]
  3. Protein Society
  4. Div Of Molecular and Cellular Bioscience
  5. Direct For Biological Sciences [0618259, 1121896] Funding Source: National Science Foundation
  6. Div Of Molecular and Cellular Bioscience
  7. Direct For Biological Sciences [0842491] Funding Source: National Science Foundation

向作者/读者索取更多资源

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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