Loth Karine, Pelupessy Philippe, Bodenhausen Geoffrey
Département de Chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris cedex 05, France.
J Biomol NMR. 2003 Oct;27(2):159-63. doi: 10.1023/a:1024979511837.
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.
