Quantitative investigation of dipole-CSA cross-correlated relaxation by ZQ/DQ spectroscopy.
- Brutscher B Laboratorium für Physikalische Chemie, ETH Zentrum, Zürich, 8092, Switzerland.
- Skrynnikov NR
- Bremi T
- BrYschweiler R
- Ernst RR
- 1998-05-02
Published in:
- Journal of magnetic resonance (San Diego, Calif. : 1997). - 1998
Anisotropy
Models, Chemical
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Ubiquitins
English
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.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1006/jmre.1997.1312
- PMID 9500898
- Persistent URL
- https://sonar.ch/global/documents/190812
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