Hydrogen-exchange stability analysis of Bergerac-Src homology 3 variants allows the characterization of a folding intermediate in equilibrium

Proceedings of the National Academy of Sciences of the United States of America

Volumn 100, Issue 10, 2003, Pages 5730-5735

  Viguera, Ana Rosa ^a   Serrano, Luis ^b  

^a UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

hairpin; Kinetics

Indexed keywords

MUTANT PROTEIN; PROTEIN KINASE P60;

ANIMAL CELL; ARTICLE; BETA SHEET; GENE INSERTION; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; HYDROGEN; HYDROGEN BONDING; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTRIN; SRC HOMOLOGY DOMAINS; THERMODYNAMICS; VARIATION (GENETICS);

ANIMALIA; INSERTION SEQUENCES;

EID: 0038286126     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0837456100     Document Type: Article

References (51)

1. Martinez, J. C. & Serrano, L. (1999) Nat. Struct. Biol. 6, 1010-1016.
2. Viguera, A. R., Martinez. J. C., Filimonov, V. V., Mateo, P. L. & Serrano, L. (1994) Biochemistry 33, 2142-2150.
3. Viguera, A. R., Jimenez, M. A., Rico, M. & Serrano, L. (1996) J. Mol. Biol. 255, 507-521.
4. Viguera, A. R. & Serrano, L. (2001) J. Mol. Biol. 311, 357-371.
5. Ramirez-Alvarado, M., Kortemme, T., Blanco, F. J. & Serrano, L. (1999) Bioorg. Med. Chem. 7, 93-103.
6. Oliveberg, M., Tan, Y. J., Silow, M. & Fersht, A. R. (1998) J. Mol. Biol. 277, 933-943.
7. Sánchez, I. E. & Kiefhaber, T. (2003) J. Mol. Biol. 325, 367-376.
8. Takei, J., Chu, R. A. & Bai, Y. (2000) Proc. Natl. Acad. Sci. USA 97, 10796-10801.
9. Fersht, A. R. (2000) Proc. Natl. Acad. Sci. USA 97, 14121-14126.
10. Chu, R. A. & Bai, Y. (2002) J. Mol. Biol. 315, 759-770.
11. Bai, Y., Sosnick, T. R., Mayne, L. & Englander, S. W. (1995) Science 269, 192-197.
12. Chamberlain, A. K., Handel, T. M. & Marqusee, S. (1996) Nat. Struct. Biol. 3, 782-787.
13. Xu, Y., Mayne, L. & Englander, S. W. (1998) Nat. Struct. Biol. 5, 774-778.
14. Llinas, M., Gillespie, B., Dahlquist, F. W. & Marqusee, S. (1999) Nat. Struct. Biol. 6, 1072-1078.
15. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., et al. (1998) Acta Crystallogr. D 54, 905-921.
16. Koradi, R., Billeter, M. & Wüthrich, K. (1996) J. Mol. Graphics 14, 51-55.
17. Englander, S. W. & Kallenbach, N. R. (1984) Q. Rev. Biophys. 16, 521-655.
18. Sibanda, B. L. & Thornton, J. M. (1985) Nature 316, 170-174.
19. Fersht, A. R. (1999) Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding (Freeman, New York).
20. Clarke, J., Itzhaki, L. S. & Fersht, A. R. (1997) Trends Biochem. Sci. 22, 284-287.
21. Plaxco, K. W., Simons, K. & Baker, D. (1998) J. Mol. Biol. 277, 985-994.
22. Eaton, W. A., Munoz, V., Hagen, S. J., Jas, G. S., Lapidus, L. J., Henry, E. R. & Hofrichter, J. (2000) Annu. Rev. Biophys. Biomol. Struct. 29, 327-359.
23. Clarke, J., Hounslow, A. M. & Fersht, A. R. (1995) J. Mol. Biol. 253, 505-513.
24. Perrett, S., Clarke, J., Hounslow, A. & Fersht, A. R. (1995) Biochemistry 34, 9288-9298.
25. Sadqi, M., Casares, S., Abril, M. A., López-Mayorga, O., Conejero-Lara, F. & Freire, E. (1999) Biochemistry 33, 8899-8906.
26. Huyghues-Despointes, B. M. P., Scholtz, J. M. & Pace, N. (1999) Nat. Struct. Biol. 6, 910-912.
27. Itzhaki, L. S., Neira, J. L. & Fersht, A. R. (1997) J. Mol. Biol. 270, 89-98.
28. Chamberlain, A. K. & Marqusee, S. (1997) Structure (London) 5, 859-863.
29. Fuentes, E. J. & Wand, A. J. (1998) Biochemistry 37, 3687-3698.
30. Fuentes, E. J. & Wand, A. J. (1998) Biochemistry 37, 9877-9883.
31. Milne, J. S., Xu, Y., Mayne, L. C. & Englander, S. W. (1999) J. Mol. Biol. 290, 811-822.
32. Arrington, C. B., Teesch, L. M. & Robertson, A. D. (1999) J. Mol. Biol. 285, 1265-1275
33. Deng, Y. & Smith, D. L. (1999) J. Mol. Biol. 294, 247-258.
34. Hoang, L., Bédard, S., Krishna, M. M. G. & Englander, S. W. (2002) Proc. Natl. Acad. Sci. USA 99, 12173-12178.
35. Raschke, T. M. & Marqusee, S. (1998) Curr. Opin. Biotechnol. 9, 80-86.
36. Parker, M. J. & Marqusee, S. (2001) J. Mol. Biol. 305, 593-602.
37. Sauder, J. M. & Roder, H. (1998) Folding Des. 3, 293-301.
38. Englander, S. W. (2000) Annu. Rev. Biophys. Biomol. Struct. 29, 213-238.
39. Perry, L. J. & Wetzel, R. (1984) Science 226, 555-557.
40. Matsumura, M., Signor, G. & Matthews, B. W. (1989) Nature 342, 291-293.
41. Munoz, V., Cronet, P. Lopez, E. & Serrano, L. (1996) Folding Des. 1, 167-178.
42. Villegas, V., Viguera, A. R., Aviles, F. X. & Serrano, L. (1996) Folding Des. 1, 29-34.
43. Spector, S., Wang, M., Carp, S. A., Robblee, J., Hendsch, Z. S., Fairman, R., Tidor, B. & Raleigh, D. P. (2000) Biochemistry 39, 872-879.
44. Khorasanizadeh, S., Peters, I. D. & Roder, H. (1996) Nat. Struct. Biol. 3, 193-205.
45. Bachmann, A. & Kiefhaber, T. (2001) J. Mol. Biol. 306, 375-386.
46. Capaldi, A. P., Kleanthous, C. & Radford, S. E. (2002) Nat. Struct. Biol. 9, 209-216.
47. Park, S. H., O'Neil, K. T. & Roder, H. (1997) Biochemistry 36, 14277-14283.
48. Hamada, D., Chiti, F., Guijarro, J. I., Kataoka, M., Taddei, N. & Dobson, C. M. (2000) Nat. Struct. Biol. 7, 58-61.
49. Inaba, K., Kobayashi, N. & Fersht, A. R. (2000) J. Mol. Biol. 302, 219-233.
50. Fukuchi, S. & Nishikawa, K. (2001) J. Mol. Biol. 309, 835-843.
51. Karshikoff, A. & Ladenstein, R. (2001) Trends Biochem. Sci. 26, 550-556.