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Measurement of 15N-13C J couplings in staphylococcal nuclease
F Delaglio1, D A Torchia, A Bax
1Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Abstract:
15N-C alpha and 15N-C' J couplings were measured for the backbone of staphylococcal nuclease, uniformly enriched with 15N and 13C. It is found that the 1JC'N coupling is similar for beta-sheet, J = 14.8 +/- 0.5 and for alpha-helix, J = 14.8 +/- 0.4 but tends to be larger for the unstructured N- and C-terminal ends of the protein (J = 15.6 +/- 0.5). On average, 1JNC alpha are smaller for alpha-helical residues (J = 9.6 +/- 0.3 Hz) compared to beta-sheet (J = 10.9 +/- 0.8 Hz) and a substantial difference is observed for 2JNC alpha in alpha-helices (J = 6.4 +/- 0.4 Hz) and beta-sheets (J = 8.3 +/- 0.8 Hz).