Journal of Physical Chemistry A, Vol.101, No.39, 7299-7303, 1997
Chemical shift tensors in peptides: A quantum mechanical study
DFT-IGLO shielding tensor calculations for the non-hydrogen nuclei in model dipeptides are presented. The behavior of the principal components, their magnitude and orientation, is investigated as a function of the dihedral angles phi and psi. For both C-alpha and amide N sites, the shielding tensor follows the molecular framework, while for C-alpha the tensor does not. Shielding tensor surfaces that span the entire Ramachandran surface (phi -180 degrees to 180 degrees, psi = -180 degrees to 180 degrees) have been constructed for both carbonyl carbon and amide nitrogen shielding tensors in a model glycyl-glycine dipeptide. The principal tensor element sigma(22) of the carbonyl shielding tensor always lies close to the C=O bond (7 degrees-9 degrees) while the sigma(11) component of the amide nitrogen shielding tensor is always slightly tilted (18 degrees-22 degrees) from the N-H bond. The effects of hydrogen bonding on the orientation and magnitude of the shielding tensor components are also investigated at selected conformations: extended, phi = 180 degrees and psi = 180 degrees; sheet, phi = -120 degrees and psi = 120 degrees; and helix, phi = -60 degrees and psi = -60 degrees. For C-alpha, calculations indicate that the shielding value along the C-alpha-H-alpha vector is very sensitive to secondary structure.