Relating dynamics to function
Article Abstract:
NMR spectroscopy is one method of studying the structural dynamics of macromolecules in solution, but the central question of how dynamics relate to function remains. Feher and Cavanagh have undertaken an NMR dynamics study characterizing movements in a response-regulator protein, SpoOF, involved in a phospho-relay signal-transduction pathway in Bacillus subtilis. They suggest that the flexibility of areas involved in protein-protein interactions may help binding of different partners, and that differing entropic contributions could contribute to binding affinity modulations.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Quantitative dynamics and binding studies of the 20S proteasome by NMR
Article Abstract:
The 670-kilodalton (kDa) 20S proteasome core particle is shown to overcome the molecular weight limitations that have always hindered quantitative nuclear magnetic resonance (NMR) spectroscopy studies of these large systems. The NMR methodology can be applied to the 20S core particle and the results have shown that it can provide insights into the supra-molecular structures having larger magnitude.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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The magic of solenoids
Article Abstract:
The technique of magic-angle spinning helps in making the nuclear magnetic resonance (NMR) spectroscopy extremely sensitive for solids, providing better signal detection due to inductive thinking.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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