Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme

Protein Engineering

Volumn 12, Issue 10, 1999, Pages 841-850

  Funahashi, Jun ^a   Takano, Kazufumi ^a   Yamagata, Yuriko ^a   Yutani, Katsuhide ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

Calorimetry; Human lysozyme; Mutant protein; Protein stability; X ray structural analysis

Indexed keywords

CARBON; LYSOZYME; MUTANT PROTEIN; NITROGEN; OXYGEN;

AMINO ACID SUBSTITUTION; ARTICLE; CALORIMETRY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENTROPY; HUMAN; HYDROGEN BOND; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 0032744714     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/12.10.841     Document Type: Article

References (58)

1. Akasako, A., Haruki, M., Oobatake, M. and Kanaya, S. (1997) J. Biol. Chem., 272, 18686-18693.
2. Blaber, M., Zhang, X.-J., Lindstrom, J.D., Pepiol, S.D., Baase, W.A. and Matthews, B.W. (1994) J. Mol. Biol., 235, 600-624.
3. Brunger, A.T. (1992) X-PLOR Manual, Version 3.1. Yale University, New Haven, CT.
4. Buckle, A.M., Henrick, K. and Fersht, A.R. (1993) J. Mol. Biol., 234, 847-860.
5. Byrne, P.M., Manuel, R.L., Lowe, L.G. and Stites, W.E. (1995) Biochemistry, 34, 13949-13960.
6. Chothia, C. (1974) Nature, 248, 338-339.
7. Chothia, C. (1976) J. Mol. Biol., 105, 1-14.
8. Dill, K.A. (1990) Biochemistry, 29, 7133-7155.
9. Doig, A.J. and Sternberg, M.J.E. (1995) Protein Sci., 4, 2247-2251.
10. Dunitz, J.D. (1994) Science, 264, 670.
11. Eisenberg, D. and McLachlan, A.D. (1986) Nature, 319, 199-203.
12. Eriksson, A.E., Baase, W.A., Zhang, X.-J., Heinz, D.W., Blaber, M., Baldwin, E.P. and Matthews, B.W. (1992) Science, 225, 178-183.
13. Eriksson, A.E., Baase, W.A. and Matthews, B.W. (1993) J. Mol. Biol., 229, 747-769.
14. Fauchere, J.-L. and Pliska, V. (1983) Eur. J. Med. Chem., 18, 369-375.
15. Funahashi, J., Takano, K., Ogasahara, K., Yamagata, Y. and Yutani, K. (1996) J. Biochem., 120, 1216-1223.
16. Kauzmann, W. (1959) Adv. Protein Chem., 14, 1-63.
17. Kellis, J.T., Nyberg, K. and Fersht, A.R. (1989) Biochemistry, 28, 4914-4922.
18. Makhatadze, G.I. and Privalov, P.L. (1993) J. Mol. Biol., 232, 639-659.
19. Makhatadze, G.I. and Privalov, P.L. (1995) Adv. Protein Chem., 47, 307-429.
20. Matsumura, M., Becktel, W.J. and Matthews, B.W. (1988a) Nature, 334, 406-410.
21. Matsumura, M., Yahanda, S., Yutani, K. and Aiba, S. (1988b) Eur. J. Biochem., 171, 715-720.
22. Matthews, B.W. (1996) FASEB J., 10, 35-41.
23. Murphy, K.P. and Freire, E. (1992) Adv. Protein Chem., 43, 313-361.
24. Myers, J.K., Pace, C.N. and Scholtz, J.M. (1997) Proc. Natl Acad. Sci. USA, 94, 2833-2837.
25. Navaza, J. (1994) Acta Crystallogr., A50, 157-163.
26. Oobatake, M. and Ooi, T. (1993) Prog. Biophys. Mol. Biol., 59, 237-284.
27. Osserman, E.F., Cole, S.J., Swan, I.D.A. and Blake, C.C.F. (1969) J. Mol. Biol., 46, 211-212.
28. Otwinowski, Z. (1990) DENZO Data Processing Package. Yale University, New Haven, CT.
29. Otzen, D.E., Rheinnecker, M. and Fersht, A.R. (1995) Biochemistry, 34, 13051-13058.
30. Pace, C.N. (1992) J. Mol. Biol., 226, 29-35.
31. Pace, C.N., Shirley, B.A., Mcnutt, M. and Gajiwala, K. (1996) FASEB J., 10, 75-83.
32. Parry, R.M., Chandan, R.C. and Shahani, K.M. (1969) Arch. Biochem. Biophys., 130, 59-65.
33. Pickett, S.D. and Sternberg, M.J. (1993) J. Mol. Biol., 231, 825-839.
34. Privalov, P.L. and Gill, S.J. (1988) Adv. Protein Chem., 39, 191-234.
35. Privalov, P.L. and Khechinashvili, N.N. (1974) J. Mol. Biol., 86, 665-684.
36. Privalov, P.L. and Makhatadze, G.I. (1993) J. Mol Biol, 232, 660-679.
37. Richards, F.M. (1977) Annu. Rev. Biophys. Bioengng, 6, 151-176.
38. Sakabe, N. (1991) Nucl. Instrum. Methods Phys. Res., A303, 448-463.
39. Sandberg, W.S. and Terwilliger, T.C. (1991) Proc. Natl Acad. Sci. USA, 88, 1706-1710.
40. Serrano, L., Kellis, J.T., Cann, P., Matouschek, A. and Fersht, A.R. (1992) J. Mol. Biol., 224, 783-804.
41. Sharp, K.A., Nicholls, A., Friedman, R. and Honig, B. (1991) Biochemistry, 30, 9686-9697.
42. Shortle, D., Stites, W.E. and Meeker, A.K. (1990) Biochemistry, 29, 8033-8041.
43. Spolar, R.S., Livingstone, J.R. and Record, M.T., Jr (1992) Biochemistry, 31, 3947-3955.
44. Takano, K., Ogasahara, K., Kaneda, H., Yamagata, Y., Fujii, S., Kanaya, E., Kikuchi, M., Oobatake, M. and Yutani, K. (1995) J. Mol. Biol., 254, 62-76.
45. Takano, K., Yamagata, Y., Fujii, S. and Yutani, K. (1997a) Biochemistry, 36, 688-698.
46. Takano, K., Funahashi, J., Yamagata, Y., Fujii, S. and Yutani, K. (1997b) J. Mol. Biol., 274, 132-142.
47. Takano, K., Yamagata, Y. and Yutani, K. (1998) J. Mol Biol., 280, 749-761.
48. Takano, K., Yamagata, Y., Kubota, M., Funahashi, J., Fujii, S. and Yutani, K., (1999a) Biochemistry, 38, 6623-6629.
49. Takano, K., Ota, M., Ogasahara, K., Yamagata, Y., Nishikawa, K. and Yutani, K. (1999b) Protein Engng, 12, 663-672.
50. Takano, K., Yamagata, Y., Funahashi, J., Hioki, Y., Kuramitsu, S. and Yutani, K. (1999c) Biochemistry, 38, in press.
51. Tanford, C. (1962) J. Am. Chem. Soc., 84, 4240-4247.
52. Vajda, S., Weng, Z., Rosenfeld, R. and DeLisi, C. (1994) Biochemistry, 33, 13977-13988.
53. Wesson, L. and Eisenberg, D. (1992) Protein Sci., 1, 227-235.
54. Wetlaufer, D.B. (1962) Adv. Protein Chem., 17, 303-390.
55. Xie, D. and Freire, E. (1994) Proteins, 19, 291-301.
56. Xu, J., Baase, W.A., Baldwin, E. and Matthews.B.W. (1998) Protein Sci., 7, 158-177.
57. Yamagata, Y., Kubota, M., Sumikawa, Y., Funahashi, K., Takano, K., Fujii, S. and Yutani, K. (1998) Biochemistry, 37, 9355-9362.
58. Yutani, K., Ogasahara, K., Tsujita, T. and Sugino, Y. (1987) Proc. Natl Acad. Sci. USA, 84, 4441-4444.