Contributions of the Large Hydrophobic Amino Acids to the Stability of Staphylococcal Nuclease

Biochemistry

Volumn 29, Issue 35, 1990, Pages 8033-8041

  Shortle, David ^a   Stites, Wesley E ^a   Meeker, Alan K ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEASE;

ARTICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; STAPHYLOCOCCUS; STRUCTURE ACTIVITY RELATION;

AMINO ACIDS; CHEMISTRY, PHYSICAL; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SUPPORT, U.S. GOV'T, P.H.S.; THERMODYNAMICS;

STAPHYLOCOCCUS;

EID: 0025005525     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00487a007     Document Type: Article

References (32)

1. Alber, T., Dao-pin, S., Nye, J. A., Muchmore, D. C., Matthews, B. W. (1987) Biochemistry 26, 3754-3758.
2. Baker, E. N., & Hubbard, R. E. (1984) Prog. Biophys. Mol. Biol. 44, 97-141.
3. Chothia, C. (1976) J. Mol. Biol. 105, 1-14.
4. Dill, K. A. (1985) Biochemistry 24, 1501-1509.
5. Fauchere, J. L., & Pliska, V. (1983) Eur. J. Med. Chem. 18, 369-375.
6. Fuchs, S., Cuatrecasas, P., & Anfinsen, C. B. (1967) J. Biol. Chem. 242, 4768-4770.
7. Guy, H. R. (1985) Biophys. J. 47, 61-70.
8. Hopp, T. P., & Woods, K. R. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 3824-3828.
9. Israelachvili, J. N. (1985) Intermolecular and Surface Forces, Academic Press, New York.
10. Kauzmann, W. (1959) Adv. Protein. Chem. 14, 1-63.
11. Kellis, J. T., Jr., Nyberg, K., Sali, D., & Fersht, A. R. (1988) Nature 333, 784-786.
12. Kunkel, T. A. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
13. Kyte, J., & Doolittle, R. F. (1982) J. Mol. Biol. 157, 105-132.
14. Loll, P. J., & Lattman, E. E. (1989) Proteins: Struct., Fund., Genet. 5, 183-201.
15. Loll, P. J., Meeker, A. M., Shortle, D., Pease, M., & Lattman, E. E. (1988) J. Biol. Chem. 263, 18190-18192.
16. Matsumura, M., Becktel, W. J., & Matthews, B. W. (1988) Nature 334, 406-410.
17. Nakai, K., Kidera, A., & Kanehisa, M. (1988) Protein Eng. 2, 93-100.
18. Nemethy, G., Leach, S. J., & Scheraga, H. A. (1966) J. Phys. Chem. 70, 998-1004.
19. Pace, C. N. (1975) Crit. Rev. Biochem. 3, 1-43.
20. Pace, C. N., Laurents, D. V., & Thomson, J. A. (1990) Biochemistry 29, 2564-2572.
21. Ponder, J. W., & Richards, F. M. (1987) J. Mol. Biol. 193, 775-791.
22. Richards, F. M. (1977) Annu. Rev. Biophys. Bioeng. 6, 151-176.
23. Richardson, J. S. (1981) Adv. Protein Chem. 34, 167-339.
24. Rose, G. D., Geselowitz, A. R., Lesser, G. J., Lee, R. H., & Zehfus, M. (1985) Science 229, 834-838.
25. Schellman, J. A. (1978) Biopolymers 17, 1305-1322.
26. Shortle, D. (1983) Gene 22, 181-189.
27. Shortle, D., & Meeker, A. K. (1986) Proteins: Struct., Funct., Genet. 1, 81-89.
28. Shortle, D., & Meeker, A. K. (1989) Biochemistry 28, 936-944.
29. Shortle, D., Meeker, A. K., & Gerring, S. L. (1989) Arch. Biochem. Biophys. 272, 103-113.
30. Sondek, J. E., & Shortle, D. (1990) Proteins: Struct., Funct., Genet. 7, 299-305.
31. Tanford, C. (1970) Adv. Protein Chem. 24, 1-95.
32. Tanford, C. (1980) The Hydrophobic Effect, Wiley & Sons, New York.