Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy.
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.
Brutscher
B
B
Laboratorium für Physikalische Chemie, ETH Zentrum, Zürich, 8092, Switzerland.
Skrynnikov
N R
NR
Bremi
T
T
BrYschweiler
R
R
Ernst
R R
RR
D016880:Anisotropy; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D014452:Ubiquitins / Q000737:chemistry*
D014452:Ubiquitins