Abstract
A novel NMR experiment allows one to characterize slow motion in macromolecules. The method exploits the fact that motions, such as rotation about dihedral angles, induce correlated fluctuations of the isotropic chemical shifts of the nuclei in the vicinity. The relaxation of two-spin coherences involving C(alpha) and Cbeta nuclei in proteins provides information about correlated fluctuations of the isotropic chemical shifts of C(alpha) and Cbeta. The difference between the relaxation rates of double- and zero-quantum coherences and is shown to be affected by cross-correlated chemical shift modulation. In ubiquitin, evidence for slow motion is found in loops or near the ends of beta-strands and alpha-helices.
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