Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange

Biochemistry

Volumn 37, Issue 11, 1998, Pages 3687-3698

  Fuentes, Ernesto J ^a   Wand, A Joshua ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CYTOCHROME; CYTOCHROME B562; HEME; HYDROGEN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CALORIMETRY; ENZYME PURIFICATION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY;

AMINO ACID SEQUENCE; CYTOCHROME B GROUP; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTONS; THERMODYNAMICS;

EID: 0032539953     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972579s     Document Type: Article

References (53)

1. Lederer, F., Glatigny, A., Bethge, P. H., Bellamy, H. D., and Matthew, F. S. (1981) J. Mol. Biol. 148, 427-48.
2. Hamada, K., Bethge, P. H., and Mathews, F. S. (1995) J. Mol. Biol. 247, 947-62.
3. Feng, Y., Sligar, S. G., and Wand, A. J. (1994) Nat. Struct. Biol. 1, 30-5.
4. Feng, Y., and Sligar, S. G. (1991) Biochemistry 30, 10150-5.
5. Hamada, D., Hoshino, M., Kataoka, M., Fink, A. L., and Goto, Y. (1993) Biochemistry 32, 10351-8.
6. Hughson, F. M., Wright, P. E., and Baldwin, R. L. (1990) Science 249, 1544-8.
7. Hughson, F. M., Barrick, D., and Baldwin, R. L. (1991) Biochemistry 30, 4113-8.
8. Cocco, M. J., and Lecomte, J. T. (1990) Biochemistry 29, 11067-72.
9. Eliezer, D., and Wright, P. E. (1996) J. Mol. Biol. 263, 531-8.
10. Falzone, C. J., Mayer, M. R., Whiteman, E. L., Moore, C. D., and Lecomte, J. T. J. (1996) Biochemistry 35, 6519-26.
11. Mayo, S. L., and Baldwin, R. L. (1993) Science 262, 873-6.
12. Kim, K. S., Fuchs, J. A., and Woodward, C. K. (1993) Biochemistry 32, 9600-8.
13. Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1994) Proteins 20, 4-14.
14. Bai, Y., and Englander, S. W. (1996) Proteins 24, 145-51.
15. Tanford, C. (1970) Adv. Protein. Chem. 24, 1-95.
16. Pace, C. N. (1975) CRC Crit. Rev. Biochem. 3, 1-43.
17. Schellman, J. A. (1978) Biopolymers 17, 1305-22.
18. Pace, C. N. (1986) Methods Enzymol. 131, 266-80.
19. Nikkila, H., Gennis, R. B., and Sligar, S. G. (1991) Eur. J. Biochem. 202, 309-13.
20. Robinson, C. R., and Sligar, S. G. (1993) Protein Sci. 2, 826-37.
21. Nozaki, Y. (1972) Methods Enzymol. 26, 43-50.
22. Kay, L. E., Keifer, P., and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-65.
23. Zhang, O., Kay, L. E., Olivier, J. P., and Forman-Kay, J. D. (1994) J. Biomol. NMR 4, 845-58.
24. Feng, Y., Wand, A. J., and Sligar, S. G. (1991) Biochemistry 30, 7711-7.
25. Press, W., Teukolsky, S., Vetterling, W., and Flannery, B. (1992) Numerical Recipes in Fortran 77. The Art of Scientific Computing, Cambridge University Press, Cambridge.
26. Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Proteins 17, 75-86.
27. Connelly, G. P., Bai, Y., Jeng, M. F., and Englander, S. W. (1993) Proteins 17, 87-92.
28. Creamer, T. P., Srinivasan, R., and Rose, G. D. (1995) Biochemistry 34, 16245-50.
29. Creamer, T. P., Srinivasan, R., and Rose, G. D. (1997) Biochemistry 36, 2832-5.
30. Pfeil, W., and Privalov, P. L. (1976) Biophvs. Chem. 4, 33-40.
31. Makhatadze, G. I., and Privalov, P. L. (1992) J. Mol. Biol. 226, 491-505.
32. Johnson, C. M., and Fersht, A. R. (1995) Biochemistry 34, 6795-804.
33. Hvidt, A., and Nielsen, S. O. (1966) Adv. Protein. Chem. 21, 287-386.
34. Englander, S. W., and Kallenbach, N. R. (1984) Q. Rev. Biophys. 16, 521-655.
35. Laidig, K. E., and Daggett, V. (1996) Folding Des. 1, 335-46.
36. Clarke, J., and Fersht, A. R. (1996) Folding Des. 1, 243-54.
37. Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Science 269, 192-7.
38. Chamberlain, A. K., Handel, T. M., and Marqusee, S. (1996) Nat. Struct. Biol. 3, 782-7.
39. Dellwo, M. J., and Wand, A. J. (1989) J. Am. Chem. Soc. 111, 4571-8.
40. Zimm, B. H., and Bragg, J. K. (1959) J. Chem. Phys. 31, 526-35.
41. Qian, H., and Schellman, J. A. (1992) J. Phys. Chem. 96, 3987-94.
42. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Protein Sci. 4, 2138-48.
43. Griko, Y. V., and Privalov, P. L. (1994) J. Mol. Biol. 235, 1318-25.
44. Aune, K. C., and Tanford, C. (1969) Biochemistry K. 4586-90.
45. Pace, C. N., and Vanderburg, K. E. (1979) Biochemistry 18, 288-92.
46. DeKoster, G. T., and Robertson, A. D. (1997) Biophys. Chem. 64, 59-68.
47. Itzhaki, L. S., Neira, J. L., and Fersht, A. R. (1997) J. Mol. Biol. 270, 89-98.
48. Privalov, P. L., and Tsalkova, T. N. (1979) Nature 280, 693-6.
49. Woodward, C. K., and Hilton, B. D. (1980) Biophys. J. 32, 561-75.
50. Schulman, B. A., and Kim, P. S. (1996) Nat. Struc. Biol. 3, 682-87.
51. Schulman, B. A., Kim, P. S., Dobson, C. M., and Redfield, C. (1997) Nat. Struct. Biol. 4, 630-34.
52. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.
53. Nicholls, A., Sharp, K. A., and Honig, B. (1991) Proteins 11, 281-96.