Detection of the sulfhydryl groups in proteins with slow hydrogen exchange rates and determination of their proton/deuteron fractionation factors using the deuterium-induced effects on the 13Cβ NMR signals

Journal of the American Chemical Society

Volumn 132, Issue 17, 2010, Pages 6254-6260

  Takeda, Mitsuhiro ^a   Jee, JunGoo ^b   Terauchi, Tsutomu ^b   Kainosho, Masatsune ^a,b  

^a NAGOYA UNIVERSITY   (Japan)

^b TOKYO METROPOLITAN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE GROUPS; AQUEOUS MEDIA; CIS-TRANS; CYS RESIDUES; DEUTERATIONS; E. COLI; EXCHANGE RATES; FRACTIONAL FACTORS; FRACTIONATION FACTORS; HYDROGEN EXCHANGE; ISOMERASES; ISOTOPE SHIFTS; ISOTOPOMERS; LOCAL STRUCTURE; NMR SIGNALS; RELATIVE INTENSITY; SIDE-CHAIN; SULFHYDRYL; SULFHYDRYL GROUPS;

AMIDES; CHEMICAL SHIFT; DEUTERIUM; ESCHERICHIA COLI;

PROTEINS;

AMINO ACID; CYSTEINE; DEUTERIUM; HYDROGEN; ISOTOPE; PEPTIDYLPROLYL ISOMERASE; PROTEIN; PROTON; THIOL GROUP;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; DEUTERON NUCLEAR MAGNETIC RESONANCE; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PROTEIN ANALYSIS; PROTON NUCLEAR MAGNETIC RESONANCE; SIGNAL TRANSDUCTION;

CARBON ISOTOPES; CYSTEINE; DEUTERIUM; HYDROGEN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEINS; PROTONS;

EID: 77951699317     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja101205j     Document Type: Article

References (35)

1. Giles, N. M., Giles, G. I., and Jacob, C. Biochem. Biophys. Res. Commun. 2003, 300, 1-4
2. Johnson, D. C., Dean, D. R., Smith, A. D., and Johnson, M. K. Annu. Rev. Biochem. 2005, 74, 247-81
3. Gregoret, L. M., Rader, S. D., Fletterick, R. J., and Cohen, F. E. Proteins 1991, 9, 99-107
4. Zhou, P., Tian, F., Lv, F., and Shang, Z. Proteins 2009, 76, 151-63
5. Jarret, R. M. and Saunders, M. J. Am. Chem. Soc. 1985, 107, 2648-2654
6. Gold, V. Adv. Phys. Org. Chem. 1969, 7, 259-331
7. Anslyn, E. V. and Dougherty, D. A. Modern Physical Organic Chemistry, University Science Books: Sausalito, CA, 2006; pp 437 - 441.
8. Balasco, J. G., Bruice, T. W., Albery, W. J., and Knowles, J. R. Biochemistry 1986, 25, 2558-2564
9. Otting, G. and Wüthrich, K. J. Am. Chem. Soc. 1989, 111, 1871-1875
10. Otting, G., Liepinsh, E., and Wüthrich, K. J. Am. Chem. Soc. 1991, 113, 4363-4364
11. Liepinsh, E., Otting, G., and Wüthrich, K. J. Biomol. NMR 1992, 2, 447-465
12. Liepinsh, E. and Otting, G. Magn. Reson. Med. 1996, 35, 30-42
13. Doreleijers, J. F., Mading, S., Maziuk, D., Sojourner, K., Yin, L., Zhu, J., Markley, J. L., and Ulrich, E. L. J. Biomol. NMR 2003, 26, 139-146
14. Takeda, M., Jee, J., Ono, M. A., Terauchi, T., and Kainosho, M. J. Am. Chem. Soc. 2009, 131, 18556-18562
15. Kainosho, M., Torizawa, T., Iwashita, Y., Terauchi, T., Ono, A. M., and Güntert, P. Nature 2006, 440, 52-57
16. Terauchi, T., Kobayashi, K., Okuma, K., Oba, M., Nishiyama, K., and Kainosho, M. Org. Lett. 2008, 10, 2785-2787
17. Connor, D. S., Klein, G. W., Jr., and Medwid, J. B. Organic Syntheses; House, H. O., Ed.; Wiley: New York, 1972; Vol. 52, pp 16.
18. Kitamura, M., Shirakawa, S., and Maruoka, K. Angew. Chem., Int. Ed. 2005, 44, 1549-1551
19. Torizawa, T., Shimizu, M., Taoka, M., Miyano, H., and Kainosho, M. J. Biomol. NMR 2004, 30, 311-325
20. Takeda, M., Ikeya, T., Güntert, P., and Kainosho, M. Nat. Protoc. 2007, 2, 2896-2902
21. Kariya, E., Ohki, S., Hayano, T., and Kainosho, M. J. Biomol. NMR 2000, 18, 75-76
22. Shaka, A. J., Keeler, J., Frenkiel, T., and Freeman, R. J. Magn. Reson. 1969, 52, 335-338
23. Takeda, M., Terauchi, T., Ono, A. M., and Kainosho, M. J. Biomol. NMR 2010, 46, 45-49
24. Hansen, P. E. Annu. Rep. NMR Spectrosc. 1983, 15, 105-234
25. Dziembowska, T., Hansen, P. E., and Rozwadowski, Z. Prog. Nucl. Magn. Reson. Spectrosc. 2004, 45, 1-29
26. Edwards, K. J., Ollis, D. L., and Dixon, N. E. J. Mol. Biol. 1997, 271, 258-265
27. Kainosho, M. and Tsuji, T. Biochemistry 1982, 21, 6273-6279
28. Kainosho, M., Nagao, H., and Tsuji, T. Biochemistry 1987, 26, 1068-1075
29. Markley, J. L. and Kainosho, M. In Stable Isotope Labeling and Resonance Assignments in Larger Proteins: NMR of Macromolecules, Roberts, G. C. K., Ed.; Oxford University Press: New York, 1993; pp 101 - 152.
30. Uchida, K., Markley, J. L., and Kainosho, M. Biochemistry 2005, 44, 11811-11820
31. Loh, S. W. and Markley, J. L. Biochemistry 1994, 33, 1029-1036
32. Harris, T. K. and Mildvan, A. S. Proteins 1999, 35, 275-282
33. Koradi, R., Billeter, M., and Wüthrich, K. J. Mol. Graph. 1996, 14, 51-55
34. All of the isotopically labeled amino acids used in this study are available from SAIL Technologies: http://www.sail-technologies.com/index.html.
35. LeMaster, D. M. Biochemistry 1996, 35, 14876-14881