NMR reveals novel mechanisms of protein activity regulation |
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| Authors: | Kalodimos Charalampos G |
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| Affiliation: | 1Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey 08854;2BioMaPS Institute for Quantitative Biology, Rutgers University, Piscataway, New Jersey 08854;3Department of Biomedical Engineering, Rutgers University, Piscataway, New Jersey 08854 |
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| Abstract: | 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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| Keywords: | NMR protein function protein regulation allosteric interactions autoinhibition |
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