Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 83
Volume 83, Issue -, Pages 291-315Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060713-035829
Keywords
high-molecular weight complexes; protein NMR; allostery; protein-substrate interactions; methyl labeling; deuteration
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Funding
- Canadian Institutes of Health Research Funding Source: Medline
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Large macromolecular assemblies, so-called molecular machines, are critical to ensuring proper cellular function. Understanding how proper function is achieved at the atomic level is crucial to advancing multiple avenues of biomedical research. Biophysical studies often include X-ray diffraction and cryo-electron microscopy, providing detailed structural descriptions of these machines. However, their inherent flexibility has complicated an understanding of the relation between structure and function. Solution NMR spectroscopy is well suited to the study of such dynamic complexes, and continued developments have increased size boundaries; insights into function have been obtained for complexes with masses as large as 1 MDa. We highlight methyl-TROSY (transverse relaxation optimized spectroscopy) NMR, which enables the study of such large systems, and include examples of applications to several cellular machines. We show how this emerging technique contributes to an understanding of cellular function and the role of molecular plasticity in regulating an array of biochemical activities.
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