title: 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.
authors.affiliation: Département de Chimie, associé au CNRS, Ecole Normale Supérieure, Paris, France.
authors.forename: M
authors.initials: M
authors.lastname: Deschamps
authors.forename: G
authors.initials: G
authors.lastname: Bodenhausen
mesh_terms: D016880:Anisotropy; D004058:Diffusion; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D025801:Ubiquitin / Q000737:chemistry*
chemical_list: D025801:Ubiquitin