Cross-correlation between a carbonyl C' chemical shift anisotropy and a long-range dipolar C'HA coupling in proteins using symmetrical reconversion

A new sequence is described to measure the cross-correlation rates between the chem. shift anisotropy of the carbonyl carbon-13 nucleus and the dipole-dipole interaction between this carbonyl and the alpha-proton in proteins. The sequence is based on the sym. reconversion principle and is insensitive to exptl. errors and to violations of the secular approxn. The cross-correlation rate depends on the backbone angle y. The advantages and limitations of the sequence are discussed. [on SciFinder (R)]

Published in:
Journal of Biomolecular NMR, 27, 2, 159-163

 Record created 2006-02-22, last modified 2018-03-17

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