Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface

Biochemistry

Volumn 38, Issue 50, 1999, Pages 16419-16423

  Loladze, Vakhtang V ^b   Ibarra Molero, Beatriz ^a,c   Sanchez Ruiz, Jose M ^c   Makhatadze, George I ^b  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b PENN STATE COLLEGE OF MEDICINE   (United States)

^c UNIVERSITY OF GRANADA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

UBIQUITIN;

AMINO ACID SUBSTITUTION; ARTICLE; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; ARGININE; ASPARAGINE; CIRCULAR DICHROISM; ELECTROSTATICS; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; LINEAR MODELS; LYSINE; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; PROTEIN FOLDING; SURFACE PROPERTIES; THERMODYNAMICS; UBIQUITINS;

EID: 0033554840     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992271w     Document Type: Article

References (28)

1. Perry, K. M., Onuffer, J. J., Gittelman, M. S., Barmat, L., and Matthews, C. R. (1989) Biochemistry 28, 7961-7968.
2. Serrano, L., Kellis, J. T., Jr., Cann, P., Matouschek, A., and Fersht, A. R. (1992) J. Mol. Biol. 224, 783-804.
3. Scholtz, J. M., and Baldwin, R. L. (1992) Annu. Rev. Biophys. Biomol. Struct. 21, 95-118.
4. Pace, C. N. (1995) Methods Enzymol. 259, 538-554.
5. Matthews, B. W. (1995) Adv. Protein Chem. 46, 249-278.
6. Bryson, J. W., Betz, S. F., Lu, H. S., Suich, D. J., Zhou, H. X., O'Neil, K. T., and DeGrado, W. F. (1995) Science 270, 935-941.
7. Smith, C. K., and Regan, L. (1995) Science 270, 980-982.
8. Cordes, M. H., Davidson, A. R., and Sauer, R. T. (1996) Curr. Opin. Struct. Biol. 6, 3-10.
9. Baldwin, R. L., and Rose, G. D. (1999) Trends Biochem. Sci. 24, 26-33.
10. Baldwin, R. L., and Rose, G. D. (1999) Trends Biochem. Sci. 24, 77-83.
11. Ramos, C. H., Kay, M. S., and Baldwin, R. L. (1999) Biochemistry 38, 9783-9790.
12. Grimsley, G. R., Shaw, K. L., Fee, L. R., Alston, R. W., Huyghues-Despointes, B. M. P., Thurlkill, R. L., Scholtz, J. M., and Pace, C. N. (1999) Protein Sci. 8, 1843-1849.
13. Ibarra-Molero, B., Loladze, V. V., Makhatadze, G. I., and Sanchez-Ruiz, J. M. (1999) Biochemistry 38, 8138-8149.
14. Tanford, C., and Kirkwood, J. G. (1957) J. Am. Chem. Soc. 79, 5333-5339.
15. Bashford, D., and Karplus, M. (1991) J. Phys. Chem. 95, 9556-9561.
16. Vijay-Kumar, S., Bugg, C. E., Wilkinson, K. D., Vierstra, R. D., Hatfield, P. M., and Cook, W. J. (1987) J. Biol. Chem. 262, 6396-6399.
17. Makhatadze, G. I., Lopez, M. M., Richardson, J. M., III, and Thomas, S. T. (1998) Protein Sci. 7, 689-697.
18. Ibarra-Molero, B., Makhatadze, G. I., and Sanchez-Ruiz, J. M. (1999) Biochim. Biophys. Acta 1429, 384-390.
19. Briggs, M. S., and Roder, H. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 2017-2021.
20. Rashin, A. A., and Honig, B. (1984) J. Mol. Biol. 173, 5I5-521.
21. Pace, C. N. (1986) Methods Enzymol. 131, 266-280.
22. Makhatadze, G. I. (1999) J. Phys. Chem. B 103, 4781-4785.
23. Stickle, D. F., Presta, L. G., Dill, K. A., and Rose, G. D. (1992) J. Mol. Biol. 226, 1143-1159.
24. Myers, J. K., and Pace, C. N. (1996) Biophys. J. 71, 2033-2039.
25. Perutz, M. F. (1978) Science 201, 1187-1191.
26. Jaenicke, R. (1999) Prog. Biophys. Mol. Biol. 71, 155-241.
27. Xiao, L., and Honig, B. (1999) J. Mol. Biol. 289, 1435-1444.
28. Makhatadze, G. I., Clore, G. M., and Gronenborn, A. M. (1995) Nat. Struct. Biol. 2, 852-855.