A J CH -Modulated 2D (HACACO)NH Pulse Scheme for Quantitative Measurement of 13 C α - 1 H α Couplings in 15 N, 13 C-Labeled Proteins

Journal of Magnetic Resonance

Volumn 140, Issue 1, 1999, Pages 281-284

  Hitchens, T Kevin ^a   McCallum, Scott A ^b   Rule, Gordon S ^a,b  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

(HACACO)NH; C H residual dipole coupling; Pulse sequence

Indexed keywords

CARBON; HYDROGEN; NITROGEN; RHO FACTOR;

ARTICLE; CHEMISTRY; HYDROGEN BOND; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SENSITIVITY AND SPECIFICITY;

CARBON; CARBON ISOTOPES; HYDROGEN; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; NITROGEN; NITROGEN ISOTOPES; RHO FACTOR; SENSITIVITY AND SPECIFICITY;

EID: 0033185791     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1999.1847     Document Type: Editorial

References (22)

1. 13 C couplings in the structure determination of magnetically oriented macromolecules in solution, Nature Struct. Biol. 4, 732-738 (1997).
2. N. Tjandra and A. Bax, Direct measurements of distances and angles in biomolecules by NMR in dilute liquid crystalline media, Science 278, 1111-1114 (1997).
3. M. R. Hansen, L. Meuller, and A. Pardi, Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions, Nature Struct. Biol. 5, 1065-1074 (1998).
4. A. Bax and N. Tjandra, High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium, J. Biomol. NMR 10, 289-292 (1997).
5. M Ottiger, F. Delaglio, and A. Bax, Measurement of J and dipolar couplings from simplified two dimensional NMR spectra, J. Magn. Reson. 131, 373-378 (1998).
6. α chemical shift anisotropy in proteins correlate with secondary structure, J. Am. Chem. Soc. 119, 9576-9577 (1997).
7. 13 C labeled proteins, J. Biomol. NMR 12, 325-332 (1998).
8. 15 N-enriched ubiquitin resulting from relaxation interference and residual dipolar coupling, J. Am. Chem. Soc. 118, 6264-6272 (1996).
9. CH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra, J. Magn. Reson. 124, 512-515 (1997).
10. N nuclei, J. Magn. Reson. B 110, 87-90 (1996).
11. W. Feng, C. B. Rios, and G. T. Montelione, Phase labeling of C-H and C-C spin-system topologies: Application in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments for determining backbone resonance assignments in proteins, J. Biomol. NMR 8, 98-104 (1996).
12. 15 N-labeled proteins, J. Biomol. NMR 9, 94-100 (1997).
13. 15 N-enriched proteins, J. Biomol. NMR 3, 185-204 (1993).
14. M. Ottiger, F. Delaglio, J. Marquardt, N. Tjandra, and A. Bax, Measurement of dipolar couplings for methylene and methyl sites in weakly oriented macromolecules and their use in structure determination, J. Magn. Reson. 134, 365-369 (1998).
15. D. M. Briercheck, T. C. Wood, T. J. Allison, J. P. Richardson, and G. S. Rule, The NMR structure of the RNA binding domain of E coli rho factor suggests possible RNA-protein interactions, Nature Struct. Biol. 5, 393-399 (1998).
16. M. L. Johnson and S. G. Frasier, Nonlinear least-squares analysis, Methods Enzymol. 117, 301-342 (1985).
17. A. J. Shaka, C. J. Lee, and A. Pines, Iterative schemes for bilinear operators: Application to spin decouplings, J. Magn. Reson. 77, 274-293 (1988).
18. A. J. Shaka, P. B. Barker, and R. Freeman, Computer optimized decoupling scheme for wide band applications and low-level operation, J. Magn. Reson. 64, 547-552 (1985).
19. 13 C] carbonyl decoupling, J. Am Chem. Soc. 114, 2108-2112 (1992).
20. D. J. States, R. A. Haberkorn, and D. J. Ruben, A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants, J. Magn. Reson. 48, 286-292 (1982).
21. 15 N HSQC experiments optimized to retain full sensitivity, J. Magn. Reson. A 102, 241-245 (1993).
22. 15 N-labeled sample, J. Am. Chem. Soc. 119, 872-880 (1997).