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

M. Deschamps (1, 2) , G. Bodenhausen (3, 4)

1 RS2E - Réseau sur le stockage électrochimique de l'énergie
2 CRMHT - Centre de recherches sur les matériaux à haute température
3 ISIC - Institut des Sciences et Ingénierie Chimiques
4 UPMC - Université Pierre et Marie Curie - Paris 6

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.

Domaines: Chimie organique

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⟩