Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data

Biochemistry

Volumn 39, Issue 18, 2000, Pages 5355-5365

  Battiste, John L ^a,b   Wagner, Gerhard ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR;

ANIMAL CELL; ARTICLE; CRYSTAL STRUCTURE; MOLECULAR MODEL; MOLECULAR WEIGHT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SPIN LABELING; STRUCTURE ANALYSIS; TRANSLATION INITIATION;

AMINO ACID SEQUENCE; CHOLIC ACIDS; DEUTERIUM; EUKARYOTIC INITIATION FACTOR-4E; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PEPTIDE INITIATION FACTORS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SPIN LABELS; YEASTS;

ANIMALIA; EUKARYOTA;

EID: 0034625121     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi000060h     Document Type: Article

References (26)

1. Kay, L. E., and Gardner, K. H. (1997) Curr. Opin. Struct. Biol. 7, 722-731.
2. Shan, X., Gardner, K. H., Muhandiram, D. R., Rao, N. S., Arrowsmith, C. H., and Kay, L. E. (1996) J. Am. Chem. Soc. 118, 6570-6579.
3. Pervushin, K., Riek, R., Wider, G., and Wuthrich, K. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 12366-71.
4. Salzmann, M., Pervushin, K., Wider, G., Senn, H., and Wuthrich, K. (1999) J. Biomol. NMR 14, 85-88.
5. Venters, R. A., Metzler, W. J., SPicer, L. D., Mueller, L., and Farmer, B. T. (1995) J. Am. Chem. Soc. 117, 9592-9593.
6. Metzler, W. J., Witteking, M., Goldfarb, V., Mueller, L., and Farmer, B. T. (1996) J. Am. Chem. Soc. 118, 6800-6801.
7. Smith, B. O., Ito, Y., Raine, A., Teichmann, S., Ben-Tovim, L., Nietlispach, D., Broadhurst, R. W., Terada, T., Kelly, M., Oschkinat, H., Shibata, T., Yokoyama, S., and Laue, E. D. (1996) J. Biomol. NMR 8, 360-368.
8. Rosen, M. K., Gardner, K. H., Willis, R. C., Parris, W. E., Pawson, T., and Kay, L. E. (1996) J. Mol. Biol. 263, 627-636.
9. Gardner, K. H., Rosen, M. K., and Kay, L. E. (1997) Biochemistry 36, 1389-1401.
10. Tjandra, N., and Bax, A. (1997) Science 278, 1111-1114.
11. Tjandra, N., Omichinski, J. G., Gronenborn, A. M., Clore, G. M., and Bax, A. (1997) Nat. Struct. Biol. 4, 732-728.
12. Kosen, P. A. (1989) Methods Enzymol. 177, 86-121.
13. Krugh, T. R. (1976) in Spin Labeling: Theory and Applications (Berliner, L. J., Ed.) pp 339-372, Academic Press, New York.
14. Gillespie, J. R., and Shortle, D. (1997) J. Mol. Biol. 268, 170-184.
15. Girvin, M. E., and Fillingame, R. H. (1994) Biochemistry 33, 665-674.
16. Gillespie, J. R., and Shortle, D. (1997) J. Mol. Biol. 268, 158-169.
17. Hubbell, W. L., Mchaourab, H. S., Altenbach, C., and Lietzow, M. A. (1996) Structure 4, 779-783.
18. Matsuo, H., Li, H., McGuire, A. M., Fletcher, C. M., Gingras, A.-C., Sonenberg, N., and Wagner, G. (1997) Nat. Struct. Biol. 4, 717-724.
19. Berliner, L. J., Grunwald, J., Hankovszky, H. O., and Hideg, K. (1982) Anal. Biochem. 119, 450-455.
20. Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293.
21. Solomon, I., and Bloembergen, N. (1956) J. Chem. Phys. 25, 261-266.
22. Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Biochemistry 35, 7692-7704.
23. Schmidt, P. G., and Kuntz, I. D. (1984) Biochemistry 23, 4261-4266.
24. Tarshis, L. C., Yan, M., Poulter, C. D., and Sacchettini, J. C. (1994) Biochemistry 33, 10871-10877.
25. Yamazaki, T., Otomo, T., Oda, N., Kyogoku, Y., and Uegaki, K. (1998) J. Am. Chem. Soc. 120, 5591-5592.
26. Xu, R., Ayers, B., Cowburn, D., and Muir, T. W. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 388-393.