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

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.
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Karine Loth, Philippe Pelupessy, Geoffrey Bodenhausen. Cross-correlation between a carbonyl C ' chemical shift anisotropy and a long-range dipolar C ' HA coupling in proteins using symmetrical reconversion. Journal of Biomolecular NMR, Springer Verlag, 2003, 27 (2), pp.159-163. ⟨10.1023/A:1024979511837⟩. ⟨hal-02128142⟩

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