Croatica Chemica Acta, Vol. 79 No. 3, 2006.
Original scientific paper
NMR h3 JNC’ Couplings Provide Comprehensive Geometrical Constraints for Protein H-bonds in Solution
Nenad Juranić
Martin C. Moncrieffe
Elena Atanasova
Slobodan Macura
Franklyn G. Prendergast
Abstract
Protein backbone H-bonds (>N–H···O–C<) show relationships between NMR h3JNC' couplings measured in solution and H-bond geometry parameters seen in X-ray crystal structures. Assuming that the solution and crystal structure of protein backbone is the same, the h3JNC' couplings can be calibrated to provide good estimates of both angular and radial H-bond parameters in a solution. The crucial premise of equality between the solution and the crystal structure of protein backbone we validated on the level of the NH-bonds orientation, by comparing the orientations inferred from X-ray crystal structures with the solution ones determined from NMR residual dipolar couplings.
Keywords
hydrogen bonding; proteins; NMR; spin-spin couplings; H-bond geometry
Hrčak ID:
5666
URI
Publication date:
12.11.2006.
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