doi: 10.1007/BF02192865.
Measurement of 15N-13C J couplings in staphylococcal nuclease
Affiliations
- PMID: 1841710
- DOI: 10.1007/BF02192865
Item in Clipboard
Measurement of 15N-13C J couplings in staphylococcal nuclease
J Biomol NMR.
1991 Nov.
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).
Similar articles
-
Measurement of two- and three-bond 13C-1H J couplings to the C delta carbons of leucine residues in staphylococcal nuclease.J Biomol NMR. 1993 May;3(3):297-306. doi: 10.1007/BF00212516. J Biomol NMR. 1993. PMID: 8358233
-
Two-dimensional NMR studies of staphylococcal nuclease. 2. Sequence-specific assignments of carbon-13 and nitrogen-15 signals from the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex.Biochemistry. 1990 Jan 9;29(1):102-13. doi: 10.1021/bi00453a012. Biochemistry. 1990. PMID: 2322533
-
Two-dimensional NMR studies of staphylococcal nuclease: evidence for conformational heterogeneity from hydrogen-1, carbon-13, and nitrogen-15 spin system assignments of the aromatic amino acids in the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex.Biochemistry. 1990 May 1;29(17):4242-53. doi: 10.1021/bi00469a029. Biochemistry. 1990. PMID: 2361141
-
Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary complex.Biochemistry. 1992 Jan 28;31(3):921-36. doi: 10.1021/bi00118a039. Biochemistry. 1992. PMID: 1731949
-
Measurement of homo- and heteronuclear J couplings from quantitative J correlation.Methods Enzymol. 1994;239:79-105. doi: 10.1016/s0076-6879(94)39004-5. Methods Enzymol. 1994. PMID: 7830604 Review. No abstract available.
Cited by
-
A protein backbone psi and phi angle dependence of 2J(N(i),C alpha(i-1)): the new NMR experiment and quantum chemical calculations.J Biomol NMR. 2005 Feb;31(2):87-95. doi: 10.1007/s10858-004-7563-7. J Biomol NMR. 2005. PMID: 15772749
-
The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy.J Am Chem Soc. 2010 Aug 11;132(31):10866-75. doi: 10.1021/ja103629e. J Am Chem Soc. 2010. PMID: 20681720 Free PMC article.
-
Alternative E.COSY techniques for the measurement of 3J(C (i) (') (-1),C (i) (beta) ) and (3) J(H (i) (N) ,C (i) (beta) ) coupling constants in proteins.J Biomol NMR. 1999 Mar;13(3):263-74. doi: 10.1023/A:1008378719908. J Biomol NMR. 1999. PMID: 20700819
-
Pulse schemes for the measurement of 3JC'C gamma and 3JNC gamma scalar couplings in 15N,13C uniformly labeled proteins.J Biomol NMR. 1997 Jun;9(4):409-22. doi: 10.1023/a:1018354712430. J Biomol NMR. 1997. PMID: 9255945
-
A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.J Biomol NMR. 2016 Dec;66(4):243-257. doi: 10.1007/s10858-016-0073-6. Epub 2016 Nov 14. J Biomol NMR. 2016. PMID: 27844185