Anisotropy of Rotational Diffusion, Dipole-Dipole Cross-Correlated NMR Relaxation and Angles between Bond Vectors in Proteins. - Archive ouverte HAL Access content directly
Journal Articles ChemPhysChem Year : 2001

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

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.

Dates and versions

hal-00825136 , version 1 (23-05-2013)

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M. Deschamps, G. Bodenhausen. Anisotropy of Rotational Diffusion, Dipole-Dipole Cross-Correlated NMR Relaxation and Angles between Bond Vectors in Proteins.. ChemPhysChem, 2001, 2 ((8-9)), pp.539-43. ⟨10.1002/1439-7641(20010917)2:8/9<539::AID-CPHC539>3.0.CO;2-M⟩. ⟨hal-00825136⟩
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