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Anisotropy of Rotational Diffusion, Dipole–Dipole Cross‐Correlated NMR Relaxation and Angles between Bond Vectors in Proteins
Author(s) -
Deschamps Michaël,
Bodenhausen Geoffrey
Publication year - 2001
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/1439-7641(20010917)2:8/9<539::aid-cphc539>3.0.co;2-m
Subject(s) - anisotropy , dipole , rotational diffusion , relaxation (psychology) , diffusion , condensed matter physics , chemistry , molecular physics , nuclear magnetic resonance , chemical physics , materials science , crystallography , physics , optics , psychology , social psychology , organic chemistry , thermodynamics
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.