Measurement of15N-13C J couplings in staphylococcal nuclease |
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Authors: | Frank Delaglio Dennis A Torchia Ad Bax |
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Institution: | (1) Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 20892 Bethesda, MD, USA;(2) Bone Research Branch, National Institute of Dental Research, National Institutes of Health, 20892 Bethesda, MD, USA |
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Abstract: | Summary
15N-C and15N-C J couplings were measured for the backbone of staphylococcal nuclease, uniformly enriched with15N and13C. It is found that theIJC'N coupling is similar for -sheet, J=14.8 ± 0.5 and for -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 are smaller for -helical residues (J=9.6 ± 0.3 Hz) compared to -sheet (J=10.9 ± 0.8 Hz) and a substantial difference is observed for2JNC in -helices (J=6.4 ± 0.4 Hz) and -sheets (J=8.3 ± 0.8 Hz).Dedicated to the memory of Professor V.F. Bystrov |
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Keywords: | 2D NMR J couplings Protein structure Isotopic labeling Triple resonance |
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