title: Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy.
abstract: A zero-quantum/double-quantum HNCO(H) constant time experiment is presented for the quantitative evaluation of dipole-CSA cross-correlated relaxation involving the 1HN, 15N, and 13C' nuclei of the peptide plane. A simple procedure that allows the extraction of cross-correlated relaxation rate constants from intensity ratios of well-resolved doublet components along omega1 is described. The experiment is demonstrated on fully 13C, 15N-labeled ubiquitin.
authors.affiliation: Laboratorium für Physikalische Chemie, ETH Zentrum, Zürich, 8092, Switzerland.
authors.forename: B
authors.initials: B
authors.lastname: Brutscher
authors.forename: N R
authors.initials: NR
authors.lastname: Skrynnikov
authors.forename: T
authors.initials: T
authors.lastname: Bremi
authors.forename: R
authors.initials: R
authors.lastname: BrYschweiler
authors.forename: R R
authors.initials: RR
authors.lastname: Ernst
mesh_terms: D016880:Anisotropy; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D014452:Ubiquitins / Q000737:chemistry*
chemical_list: D014452:Ubiquitins