Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments

Journal of the American Chemical Society

Volumn 127, Issue 13, 2005, Pages 4554-4555

  Atreya, Hanudatta S ^a   Eletsky, Alexander ^a   Szyperski, Thomas ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

ALPHA HELIX; ARTICLE; CHEMICAL BOND; NUCLEAR MAGNETIC RESONANCE; POLARIZATION; PROTEIN ANALYSIS; STRUCTURE ANALYSIS;

FOURIER ANALYSIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS;

EID: 16844363245     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja042562e     Document Type: Article

References (27)

1. Cavanagh, J.; Fairbrother, W. J.; Palmer, A. G.; Skelton, N. J. Protein NMR Spectroscopy; Academic Press: San Diego, CA, 1996.
2. (a) Szyperski, T.; Braun, D.; Fernandez, C.; Bartels, C.; Wuthrich, K. J. Magn. Reson. B 1995, 109, 229-233.
3. (b) Konrat, R.; Yang, D.; Kay, L. E. J. Biomol. NMR 1999, 15, 309-313.
4. Szyperski, T.; Yeh, D. C.; Sukumaran, D. K.; Moseley, H. N. B.; Montelione, G. T. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 8009-8014.
5. (a) Kim, S.; Szyperski, T. J. Am. Chem. Soc. 2003, 125, 1385-1393.
6. (b) Kim, S.; Szyperski, T. J. Biomol. NMR 2004, 28, 117-130.
7. (c) Atreya, H. S.; Szyperski, T. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 9642-9647.
8. (a) Szyperski, T.; Wider, G.; Bushweller, J. H.; Wüthrich, K. J. Am. Chem. Soc. 1993, 115, 9307-9308.
9. (b) Brutscher, B.; Simorre, J. P.; Caffrey, M. S.; Marion, D. J. Magn. Reson. B 1995, 109, 238-242.
10. (c) Szyperski, T.; Braun, D.; Banecki, B.; Wüthrich, K. J. Am. Chem. Soc. 1996, 118, 8147-8148.
11. (d) Löhr, F.; Rüterjans, H J. Biomol. NMR 1995, 6, 189-195.
12. (e) Szyperski, T.; Banecki, B.; Braun, D.; Glaser, R. W. J. Biomol. NMR 1998, 11, 387-405.
13. (a) Bodenhausen, G.; Ernst, R. R. J. Magn. Reson. 1981, 45, 367-373.
14. (b) Atreya, H. S.; Szyperski, T. Methods Enzymol. 2005, 394, 78-108.
15. (c) Kupce, E.; Freeman, R. J. Am. Chem. Soc. 2003, 125, 13958-13959.
16. (d) Coggins, B. E.; Venters, R. A.; Zhou, P. J. Am. Chem. Soc. 2004, 126, 1000-1001.
17. (a) Pervushin, K.; Riek, R.; Wider, G.; Wuthrich, K. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 12366-12371.
18. (b) Pervushin, K.; Vogeli, B.; Eletski, A. J. Am. Chem. Soc. 2002, 124, 12898-12902.
19. Gardner, K. H.; Kay, L. E. Annu. Rev. Biophys. Biomol. Struct. 1998, 27, 307-318.
20. α}{CON}HN (Figures S5 and S6) is often more sensitive then the out-and-back implementation.
21. (a) Hoch, J. C.; Stern, A. S. NMR Data Processing; Wiley-Liss: New York, 1996.
22. (b) Rovnyak, D.; Frueh, D. P.; Sastry, M.; Sun, Z.-Y. J.; Stern, A. S.; Hich, J. C.; Wagner, G. J. Magn. Reson. 2004, 170, 15-21.
23. Montelione, G. T.; Zheng, D.; Huang, Y.; Gunsalus, C.; Szyperski, T. Nat. Struct. Biol. 2002, 7, 982-984.
24. Tashiro, M.; Tejero, R.; Zimmerman, D. E.; Celda, B.; Nilsson, B.; Montelione, G. T. J. Mol. Biol. 1997, 272, 573-590.
25. 15N), accurately defined in (3,2)D HNNCO.
26. 2FT experiments described in this publication can provide a total of 24 sequential walks.
27. Sorgen P. L.; Hu, Y.; Guan, L.; Kaback, H. R.; Girvin, M. E. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 14037-14040.