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Measurement of15N-13C J couplings in staphylococcal nuclease
Authors:Frank Delaglio  Dennis A Torchia  Ad Bax
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
Abstract:Summary 15N-Cagr and15N-Cprime J couplings were measured for the backbone of staphylococcal nuclease, uniformly enriched with15N and13C. It is found that theIJC'N coupling is similar for beta-sheet, J=14.8 ± 0.5 and for agr-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,1JNCagr are smaller for agr-helical residues (J=9.6 ± 0.3 Hz) compared to beta-sheet (J=10.9 ± 0.8 Hz) and a substantial difference is observed for2JNCagr in agr-helices (J=6.4 ± 0.4 Hz) and beta-sheets (J=8.3 ± 0.8 Hz).Dedicated to the memory of Professor V.F. Bystrov
Keywords:2D NMR  J couplings  Protein structure  Isotopic labeling  Triple resonance
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