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Quantitative Investigation of Dipole–CSA Cross-Correlated Relaxation by ZQ/DQ Spectroscopy by B. Brutscher; N.R. Skrynnikov; T. Bremi; R. Brüschweiler; R.R. Ernst is a Chemistry article available to read on EtoBox.

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A zero-quantum/double-quantum HNCO(H) constant time exconsisting of the 1 H N , 15 N, and 13 C nuclei of the peptide periment is presented for the quantitative evaluation of dipoleplane in proteins. A key feature of the experiment is that CSA cross-correlated relaxation involving the 1 H N , 15 N, and 13 C the cross-correlated relaxation effects of interest are maninuclei of the peptide plane. A simple procedure that allows the fested as differential monoexponential relaxation in the two extraction of cross-correlated relaxation rate constants from intencomponents of the normally well-resolved 15 N-1 H N doublet. sity ratios of well-resolved doublet components along v 1 is de-This allows a simple and robust procedure for the extraction scribed. The experiment is demonstrated on fully 13 C, 15 N-labeled of cross-correlation parameters, which is well suited to pracubiquitin. ᭧ 1998 Academic Press tical applications.

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Author

B. Brutscher; N.R. Skrynnikov; T. Bremi; R. Brüschweiler; R.R. Ernst

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 1090-7807)

Published

1998

Language

EN

Field

Chemistry (Physical Sciences)