Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks

Journal of Molecular Biology

Volumn 268, Issue 1, 1997, Pages 198-208

  Johnson, Christopher M ^a   Oliveberg, Mikael ^a   Clarke, Jane ^a   Fersht, Alan R ^a  

^a MRC CENTRE FOR PROTEIN ENGINEERING   (United Kingdom)

Author keywords

Denaturation; Enthalpy; Entropy; Folding; Thermodynamics

Indexed keywords

BARNASE; CYSTEINE; CYSTINE; ENZYME; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENTHALPY; ENTROPY; ENZYME DENATURATION; ENZYME STABILITY; PH; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

EID: 0031585997     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0928     Document Type: Article

References (37)

1. Becktel W. J., Schellman J. A. Protein stability curves. Biopolymers. 26:1987;1859-1877.
2. Betz S. F. Disulfide bonds and the stability of globular proteins. Protein Sci. 2:1993;1551-1558.
3. Clarke J., Fersht A. R. Engineering disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry. 32:1993;4322-4329.
4. Clarke J., Hounslow A. M., Bycroft M., Fersht A. R. Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways. Proc. Natl Acad. Sci. USA. 90:1993;9837-9841.
5. Clarke J., Henrick K., Fersht A. R. Disulfide mutants of barnase I: changes in stability and structure assessed by biophysical methods and X-ray crystallography. J. Mol. Biol. 253:1995a;493-504.
6. Clarke J., Hounslow A. M., Fersht A. R. Disulfide mutants of barnase II: changes in structure and local stability identified by hydrogen exchange. J. Mol. Biol. 253:1995b;505-513.
7. Cooper A., Eyles S. J., Radford S. E., Dobson C. M. Thermodynamic consequences of the removal of a disulphide bridge from hen lysozyme. J. Mol. Biol. 225:1992;939-943.
8. Doig A. J., Williams D. H. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 217:1991;389-398.
9. Dunitz J. D. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2:1995;709-712.
10. Flory P. J. Theory of elastic mechanisms in fibrous proteins. J. Am. Chem. Soc. 78:1956;5222-5235.
11. Gomez J., Hilser V., Xie D., Freire E. The heat capacity of proteins. Proteins: Struct. Funct. Genet. 22:1995;404-412.
12. Griko Y. V., Makhatadze G. I., Privalov P. L., Hartley R. W. Thermodynamics of barnase unfolding. Protein Sci. 3:1994;669-676.
13. Horovitz A., Serrano L., Avron B., Bycroft M., Fersht A. R. Strength and cooperativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216:1990;1031-1044.
14. Jencks W. Catalysis in Chemistry and Enzymology. 1969;McGraw-Hill, London.
15. Johnson C. M., Fersht A. R. Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea. Biochemistry. 34:1995;6795-6804.
16. Katz B. A., Kossiakoff A. The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. J. Biol. Chem. 261:1986;15480-15485.
17. Kuroki R., Inaka K., Taniyama Y., Kidokoro S., Matsushima M., Kikuchi M., Yutani K. Enthalpic stabilization of a mutant human lysozyme lacking a disulphide bridge between cysteine-77 and cysteine-95. Biochemistry. 31:1992;8323-8328.
18. Loewenthal R., Sancho J., Fersht A. R. Histidine-aromatic interactions in barnase: elevation of histidine pKa and contribution to protein stability. J. Mol. Biol. 224:1992;759-770.
19. Lumry R., Rajender S. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers. 9:1970;1125-1227.
20. Martinez J. C., El Harrous M., Filimonov V. V., Mateo P. L., Fersht A. R. A calorimetric study of the thermal stability of barnase and its interaction with 3′GMP. Biochemistry. 33:1994;3919-3926.
21. Matouschek A., Matthews J. A., Johnson C. M., Fersht A. R. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. Protein. Eng. 7:1994;1089-1095.
22. Oliveberg M., Vuilleumier S., Fersht A. R. Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. Biochemistry. 33:1994;8826-8832.
23. Oliveberg M., Arcus V., Fersht A. R. pKa values of carboxyl groups in the native and denatured states of barnase: the pKa values of the denatured state are on average 0.4 units lower than those of model compounds. Biochemistry. 34:1995;9424-9433.
24. Pace C. N., Grimsley G. R., Thomson J. A., Barnett B. J. Conformational stability and activity of ribonuclease T1 with zero, one and two intact disulphide bonds. J. Biol. Chem. 263:1988;11820-11825.
25. Poland D. C., Scheraga H. A. Statistical mechanics of noncovalent bonds in polyamino acids. VIII. Covalent loops in proteins. Biopolymers. 3:1965;379-399.
26. Privalov P. L. Stability of proteins. Advan. Protein Chem. 33:1979;167-236.
27. Privalov P. L., Makhatadze G. I. Heat capacity of proteins II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects. J. Mol. Biol. 213:1990;385-391.
28. Privalov P. L., Tiktopulo E. I., Venyaminov S. Y., Griko Y. V., Makhatadze G. I., Khechinashvili N. N. Heat capacity and conformation of proteins in the denatured state. J. Mol. Biol. 205:1989;737-750.
29. Robertson A. D., Baldwin R. L. Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry. 30:1991;9907-9914.
30. Roder H., Wagner G., Wütrich K. Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor. Biochemistry. 24:1985;7407-7411.
31. Sali D., Bycroft M., Fersht A. R. Stabilization of protein structure by interaction of an alpha-helix dipole with a charged side chain. Nature. 335:1988;496-500.
32. Sanz J. M., Johnson C. M., Fersht A. R. The A-state of barnase. Biochemistry. 33:1994;11189-11199.
33. Serrano L., Horovitz A., Avron B., Bycroft M., Fersht A. R. Estimating the contribution of engineered surface electrostatic interactions to protein stability using double-mutant cycles. Biochemistry. 29:1990;9343-9352.
34. Sturtevant J. M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl Acad. Sci. USA. 74:1977;2236-2240.
35. Tidor B., Karplus M. The contribution of cross-links to protein stability: a normal mode analysis of the configurational entropy of the native state. Proteins: Struct. Funct. Genet. 15:1993;71-79.
36. Wetzel R. Harnessing disulphide bonds using protein engineering. Trends Biochem. Sci. 12:1987;478-482.
37. Wyman J. Linked functions and reciprocal effects in hemoglobin: a second look. Advan. Protein Chem. 19:1964;223-286.