Anisotropy of Rotational Diffusion, Dipole-Dipole Cross-Correlated NMR Relaxation and Angles between Bond Vectors in Proteins.
 

Anisotropy of Rotational Diffusion, Dipole-Dipole Cross-Correlated NMR Relaxation and Angles between Bond Vectors in Proteins.

Related Articles Anisotropy of Rotational Diffusion, Dipole-Dipole Cross-Correlated NMR Relaxation and Angles between Bond Vectors in Proteins.

Chemphyschem. 2001 Sep 17;2(8-9):539-43

Authors: Deschamps M, Bodenhausen G

Abstract
Cross correlations between the fluctuations of dipolar (13) C(?) -(1) H(?) interactions yield information about the relative orientation of successive (13) C(?) -(1) H(?) 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.


PMID: 23686993 [PubMed - in process]



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