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Cross-correlation between a carbonyl C' chemical shift anisotropy and a long-range dipolar C'HA coupling in proteins
Karine Loth1, Philippe Pelupessy, Geoffrey Bodenhausen
1Département de Chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris cedex 05, France.
Journal of Biomolecular NMR
|August 13, 2003
Abstract:
A new sequence is described to measure the cross-correlation rates between the chemical 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 symmetrical reconversion principle and is insensitive to experimental errors and to violations of the secular approximation. The cross-correlation rate depends on the backbone angle psi. The advantages and limitations of the sequence are discussed.