A pentapeptide model for an early folding step in the refolding of staphylococcal nuclease: The role of its turn propensity

Biopolymers

Volumn 41, Issue 2, 1997, Pages 181-191

  Ramakrishna, V ^a   Sasidhar, Y U ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; ENTROPY; HYDROGEN; ION EXCHANGE; POLYPEPTIDES; PROTEINS; PROTONS; TEMPERATURE;

FOLDING; OVERHAUSER EFFECT; PENTAPEPTIDE MODEL; STAPHYLOCOCCAL NUCLEASE;

ENZYMES;

BACTERIAL ENZYME; DEUTERIUM; NUCLEASE;

ARTICLE; ENTROPY; HYDROGEN BOND; NOMENCLATURE; PROTEIN FOLDING; SEQUENCE ANALYSIS; STAPHYLOCOCCUS; STRUCTURE ANALYSIS;

MICROCOCCAL NUCLEASE; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN FOLDING;

EID: 0031080855     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(199702)41:2<181::AID-BIP5>3.0.CO;2-P     Document Type: Article

References (48)

1. Kim, P. S. & Baldwin, R. L. (1982) Ann. Rev. Biochem. 51, 459-489.
2. Kim, P. S. & Baldwin, R. L. (1990) Ann. Rev. Biochem. 59, 631-660.
3. Karplus, M. & Weaver, D. L. (1979) Biopolymers 18, 1421-1437.
4. Karplus, M. & Weaver, D. L. (1994) Protein Sci. 3, 650-668.
5. Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A. & Wright, P. E. (1988) J. Mol. Biol. 201, 161-200.
6. Dyson, H. J., Rance, M., Houghten, R. A., Wright, P. E. & Lerner, R. A. (1988) J. Mol. Biol. 201, 201-217.
7. Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A. & Wright, P. E. (1992) J. Mol. Biol. 226, 795-817.
8. Waltho, J. P., Feher, V. A., Lerner, R. A. & Wright, P. E. (1989) FEBS Lett. 250, 400-404.
9. Chandrasekhar, K., Profy, A. T. & Dyson, H. J. (1991) Biochemistry 30, 9187-9194.
10. Jennings, P. A. & Wright, P. E. (1993) Science 262, 892-896.
11. Hughson, F. M., Wright, P. E. & Baldwin, R. L. (1990) Science 249, 1544-1548.
12. Wu, L. C., Laub, P. B., Elove, G. A., Carey, J. & Roder, H. (1993) Biochemistry 32, 10,271-10,276.
13. Roder, H., Elove, G. A. & Englander, S. W. (1988) Nature (London) 335, 700-704.
14. Lewis, P. N., Momany, F. A. & Scheraga, H. A. (1971) Proc. Natl. Acad. Sci. USA 68, 2293-2297.
15. Zimmerman, S. J. & Scheraga, H. A. (1977) Proc. Natl. Acad. Sci. USA 74, 4126-4129.
16. Dyson, H. J., Cross, K. J., Houghten, R. A., Wilson, I. A., Wright, P. E. & Lerner, R. A. (1985) Nature (London) 318, 480-483.
17. Jacob, M. O. & Fox, R. O. (1994) Proc. Natl. Acad. Sci. USA 91, 449-453.
18. Loll, P. J. & Lattman, E. E. (1989) Proteins Struct. Fund. Genet. 5, 183-201.
19. Bax, A. & Davis, D. G. (1985) J. Magn. Res. 63, 207-213.
20. Bax, A. & Davis, D. G. (1985) J. Magn. Res. 65, 355-360.
21. Wokaun, A. & Ernst, R. R. (1977) Chem. Phys. Lett. 52, 407-412.
22. Piantini, V., Sorensen, O. W. & Ernst, R. R. (1982) J. Am. Chem. Soc. 104, 6800-6801.
23. Shaka, A. J. & Freeman, R. (1983) J. Magn. Reson. 51, 169-173.
24. Pullman, B. & Pullman, A. (1974) Adv. Protein Chem. 28, 347-526.
25. Pullman, B. & Saran, A. (1976) Prog. Nucleic Acid. Res. Mol. Biol. 18, 215-322, and references cited therein for PCILO methodology.
26. Hosur, R. V., Chary, K. V. R., Saran, A., Govil, G. & Miles, H. T. (1990) Biopolymers 29, 953-959.
27. Nandel, F. S., Ahluwalia, A. & Kaur, A. (1995) Int. J. Quantum Chem. 55, 61-69.
28. Saran, A., Dhingra, M. M. & Sasidhar, Y. U. (1991) J. Mol. Struct. (Theochem.) 233, 315-334.
29. Tvaroska, I. (1989) Int. J. Quantum Chem. 35, 141-151.
30. Guantieri, V., Tamburo, A. M., Cabrol, D., Broch, H. & Vasilescu, D. (1987) Int. J. Peptide Protein Res. 29, 216-230.
31. Momany, F. A., McGuire, R. F., Burgess, A. W. & Scheraga, H. A. (1975) J. Phys. Chem. 79, 2361-2381.
32. Nemethy, G., Pottle, M. S. & Scheraga, H. A. (1983) J. Phys. Chem. 87, 1883-1887.
33. Wuthrich, K., Billeter, M. & Braun, W. (1984) J. Mol. Biol. 180, 715-740.
34. Billeter, M., Braun, W. & Wuthrich, K. (1982) J. Mol. Biol. 155, 321-346.
35. Dyson, H. J. & Wright, P. E. (1991) Ann. Rev. Biophys. Biophys. Chem. 20, 519-538.
36. Neuhaus, D. & Keeler, J. (1986) J. Magn. Reson. 68, 568-574.
37. Lewis, P. N., Momany, F. A. & Scheraga, H. A. (1973) Biochem. Biophys. Acta 303, 211-219.
38. Oka, M., Montelione,G. T. & Schrega, H. A. (1984) J. Am. Chem. Soc. 106, 7959-7969.
39. Chou, P. Y. & Fasman, G. D. (1977) J. Mol. Biol. 115, 135-175.
40. Deleage, G., Clerc, F. F., Roux, B. & Gautheron, D. C. (1988) CABIOS 4, 351-356.
41. Deleage, G., Clerc, F. F. & Roux, B. (1989) CABIOS 5, 159-160.
42. Garnier, O. & Robson (1978) J. Mol. Biol. 120, 97-120.
43. Kemmink, J., van Mierlo, C. P. M., Scheck, R. M. & Creighton, T. E. (1993) J. Mol. Biol. 230, 312-322.
44. Kemmink, J. & Creighton, T. E. (1995) J. Mol. Biol. 245, 251-260.
45. Ptitsyn, O. B., Finkelstein, A. V. & Falk, P. (1979) FEBS Lett. 101, 1-5.
46. Branden, C. & Tooze, J. (1991) in Introduction to Protein Structure, Garland Publishing, New York & London, pp. 11-31.
47. Bernstein, F. C., Koetzle, T. F., Williams, G. J., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T. & Tasumi, M. (1977) J. Mol. Biol. 112, 535-542.
48. Sayle, R. & Milner-White, E. J. (1995) Trends Biochem. Sci. 20, 333-379.