Dm. Lemaster et al., DIFFERENTIAL DEUTERIUM-ISOTOPE SHIFTS AND ONE-BOND H-1-C-13 SCALAR COUPLINGS IN THE CONFORMATIONAL-ANALYSIS OF PROTEIN GLYCINE RESIDUES, Journal of biomolecular NMR, 4(6), 1994, pp. 863-870
The one-bond deuterium isotope shift effect for glycine C-alpha resona
nces exhibits a conformational dependence comparable to that of the co
rresponding (1)J(HC) scalar coupling in both magnitude (similar to 11
Hz at 14.1 T) and dihedral angle dependence. The similarity in the con
formational dependence of the (1)J(HC) and deuterium isotope shift val
ues suggests a common physical basis. Given the known distribution of
(phi,psi) main-chain dihedral angles for glycine residues, the deuteri
um isotope shifts and the (1)J(HC) scalar couplings can determine conf
ormations in the left- and right-handed helical-to-bridge regions of t
he (phi,psi) plane to an accuracy of approximately 13 degrees. In the
absence of stereochemical assignments, the differential deuterium isot
ope shifts and the (1)J(HC) scalar couplings can be combined with limi
ted independent structural information (e.g., the sign of phi) to dete
rmine the chirality of the deuterium substitution.