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NMR reveals novel mechanisms of protein activity regulation
Author(s) -
Kalodimos Charalampos G.
Publication year - 2011
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.614
Subject(s) - nuclear magnetic resonance spectroscopy , biomolecule , supramolecular chemistry , chemistry , characterization (materials science) , transverse relaxation optimized spectroscopy , fluorine 19 nmr , nanotechnology , chemical physics , materials science , molecule , stereochemistry , biochemistry , organic chemistry
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.