A water mediated electrostatic interaction gives thermal stability to the "tail" region of the GrpE protein from E. coli

Protein Journal

Volumn 26, Issue 4, 2007, Pages 239-245

  Mehl, Andrew F ^a   Demeler, Borries ^b   Zraikat, Afaq ^a  

^a KNOX COLLEGE   (United States)

^b Mays Cancer Center at UT Health San Antonio   (United States)

Author keywords

Electrostatic interactions; GrpE; Oligomerization; Protein stability; Salt bridge

Indexed keywords

BACTERIAL PROTEIN; GRPE PROTEIN; UNCLASSIFIED DRUG; WATER;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; ELECTRICITY; ESCHERICHIA COLI; NONHUMAN; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STATISTICAL SIGNIFICANCE; THERMOSTABILITY; ULTRACENTRIFUGATION;

CIRCULAR DICHROISM; DIMERIZATION; ELECTROSTATICS; ESCHERICHIA COLI PROTEINS; HEAT; HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SALTS; TEMPERATURE; THERMODYNAMICS; WATER;

EID: 34250655721     PISSN: 15723887     EISSN: 15734943     Source Type: Journal    
DOI: 10.1007/s10930-006-9065-9     Document Type: Article

References (25)

1. Bjork A., Dalhus B., Mantzilas D., Sirevag R., Eijsink V. G. H. (2004). J. Mol. Biol. 341: 1215-1226
2. Bogin O., Levin I., Hacham Y., Tel-or S., Peretz M., Frolow F., Burstein Y. (2002). Protein Sci. 11: 2561-2574
3. Bradford M. M. (1976). Anal. Biochem. 72: 248-254
4. Demeler B. (2005). In: Scott D. E., Harding S. E., Rowe A. J. (eds.), Modern Analytical Ultracentrifugation: Techniques and Methods Royal Society of Chemistry, UK, pp. 210-229
5. Demeler, B. (2006). UltraScan 7.3. University of Texas Health Science Center at San Antonio, Dept. of Biochemistry. http://www.ultrascan.uthscsa.edu
6. Durchschlag H. (1986). In: Hinz H. J. (Ed.), Thermodynamic Data for Biochemistry and Biotechnology, Springer-Verlag, New York, pp. 45-128
7. Gelinas A. D., Langsetmo K., Toth J., Bethoney K. A., Stafford W. F., Harrison C. J. (2002). J. Mol. Biol. 323: 131-142
8. Gill S. C., von Hippel P. H. (1989). Anal. Biochem. 182: 319-326
9. Grimshaw J. P. A., Jelesarov I., Schonfeld H-J., Christen P. (2001). J. Biol. Chem. 9: 6098-6104
10. Grimshaw J. P. A., Jelesarov I., Siegenthaler R. K., Christein P. (2003). J. Biol. Chem. 278: 19048-19053
11. Harrison C. J., Hayer-Hartl M., Di Liberto M., Hartl F.-U., Kuriyan J. (1997). Science 276: 431-435
12. Hendsch Z. S., Tidor B. (1994). Protein Sci. 3: 211-226
13. Honig B., Nicholls A. (1995). Science 268: 1144-1149
14. Ikura T., Urakubo Y., Ito N. (2004). Chem. Phys. 307: 111-119
15. Koradi R., Billeter M., Wuthrich K. (1996). J. Mol. Graphics 14: 51-55
16. Laue T. M., Shah B. D., Ridgeway T. M., Pelletier S. L. (1992). In: Harding S. E., Rowe A. J., Horton C. J. (eds.), Analytical Ultracentrifugation in Biochemistry and Polymer Science, Royal Society of Chemistry, Cambridge, pp. 90-125
17. Luisi D. L., Snow C. D., Lin J.-J., Hendsch Z. S., Tidor B., Raleigh D. P. (2003). Biochemistry 42: 7050-7060
18. Matheson I. B. C., Parkhurst L. J., Desa R. J. (2004). Methods Enzymol. 384: 18-39
19. Mehl A. F., Heskett L. D., Jain S. S., Demeler B. (2003). Protein Sci. 12: 1205-1215
20. Mehl A. F., Heskett L. D., Neal K. M. (2001). Biochem. Biophys. Res. Commun. 282: 562-569
21. Natesh R., Manikandan K., Bhanumoorthy P., Viswamitra M. A., Ramakumar S. (2003). Acta Cryst. D59: 105-117
22. Siegenthaler R. K., Christen P. (2005). J. Biol. Chem. 280: 14395-14401
23. Strop P., Mayo S. L. (2000). Biochemistry 39: 1251-1255
24. Vieille C., Zeikus G. J. (2001). Microbiol. Mol. Biol. Rev. 65: 1-43
25. Wu B., Ang D., Snavely M., Georgopolous C. (1994). J. Bact. 176: 6965-6973