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Conformation and Hydrogen Bonding Influence on the CSA Tensor of Models for Peptide Backbone Atoms

The H-1, C-13 and N-15 CSA tensors in peptide models have been investigated with respect to their dependence on conformational and hydrogen bonding parameters. Backbone torsion dependencies are visualized by way of Ramachandran-type diagrams for a dipeptide model. For each backbone atom the CSA tensor was analyzed by itself and, additionally, in the context of cross-correlated relaxation with selected dipole-dipole interactions. This was to allow comparison to both solid state and liquid state (cross-correlation) NMR experiments. The influence of hydrogen bond distance on H-1, C-13 and N-15 CSA tensors prevails over any effects from hydrogen bonding angles. The relative influences of conformation and hydrogen bonding on the CSA tensors and cross correlation rates will be compared.

NMR; CSA; conformation; hydrogen bonding

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