ISSN:
1573-5001
Keywords:
2D NMR
;
J couplings
;
Protein structure
;
Isotopic labeling
;
Triple resonance
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary 15N-Cα 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 β-sheet, J=14.8 ± 0.5 and for α-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,1JNCα are smaller for α-helical residues (J=9.6 ± 0.3 Hz) compared to β-sheet (J=10.9 ± 0.8 Hz) and a substantial difference is observed for2JNCα in α-helices (J=6.4 ± 0.4 Hz) and β-sheets (J=8.3 ± 0.8 Hz).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02192865
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