A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational amplitudes, and rotational correlation coefficients with different NMR relaxation parameters have been obtained. Auto- and cross-correlation spectral densities are considered, and it is shown that proton-coupled 13C NMR relaxation measurements allow detailed motional information to be obtained.
Daragan
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VA
Biomedical Engineering Center, 4-225 Millard Hall, University of Minnesota, 435 Delaware St., S.E., Minneapolis, Minnesota 55455, USA.
Mayo
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KH
D008433:Mathematics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results
D011506:Proteins