Anisotropic Dynamics of Protein Side Chain NH(2) Groups Revealed through Analysis of (2)H and (15)N NMR Relaxation Rates
Although nuclear magnetic resonance (NMR) spectroscopy is powerful for protein dynamics investigations, the anisotropy of internal motions has been difficult to analyze with NMR. In principle, NMR order parameters for multiple bond vectors fixed on the same plane can reveal the anisotropy of internal motions. We investigated the anisotropic dynamics of protein asparagine (Asn) and glutamine (Gln) side chain NH(2) groups using ²H and ^(15)N NMR relaxation rates. Hindered rotations about the C-N...
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