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Updated: May 11, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Anisotropy of rotational diffusion, dipole-dipole cross-correlated NMR relaxation and angles between bond vectors in
1Département de Chimie, associé au CNRS, Ecole Normale Supérieure, Paris, France.
Abstract:
Cross correlations between the fluctuations of dipolar (13)C(α)-(1)H(α) interactions yield information about the relative orientation of successive (13)C(α)-(1)H(α) bond vectors in proteins, in turn providing a direct handle on their structure and dynamics in solution. However, overall anisotropic reorientation must be taken into account in the interpretation of cross-correlation rates. The protein shown, human ubiquitin, has amino acid residues in white where the cross-correlation rates deviate from those predicted for a rigid structure.
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