Pressure/temperature effects on protein flexibilty from acrylamide quenching of protein phosphorescence

Journal of Molecular Biology

Volumn 291, Issue 4, 1999, Pages 955-964

  Cioni, Patrizia ^a   Strambini, Giovanni B ^a  

^a CNR Consiglio Nazionale delle Ricerche   (Italy)

Author keywords

Acrylamide; Phosphorescence; Protein dynamics; Quenching; Tryptophan

Indexed keywords

ACRYLAMIDE; ALCOHOL DEHYDROGENASE; ALKALINE PHOSPHATASE; PROTEIN;

ARTICLE; CONTROLLED STUDY; DIFFUSION; ENZYME ACTIVATION; HYDROSTATIC PRESSURE; NONHUMAN; PHOSPHORESCENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE; THERMODYNAMICS;

EID: 0033609806     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3010     Document Type: Article

References (33)

1. Carter J. V., Knox D. G., Rosenberg A. Pressure effects on folded proteins in solution. J. Biol. Chem. 253:1978;1947-1953.
2. Chalikian T. V., Totrov M., Abagyan R., Breslauer K. J. The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data. J. Mol. Biol. 260:1996;588-603.
3. Cioni P., Strambini G. B. Pressure effects on protein flexibility: monomeric proteins. J. Mol. Biol. 242:1994;291-301.
4. Cioni P., Strambini G. B. Pressure effects on the structure of oligomeric proteins prior to subunit dissociation. J. Mol. Biol. 263:1996;789-799.
5. Cioni P., Strambini G. B. Acrylamide quenching of protein phosphorescence as a monitor of structural fluctuations in the globular fold. J. Am. Chem. Soc. 120:1998;11749-11757.
6. Eftink M. R. Fluorescence quenching: theory and applications. Lakowicz J. R. Topics in Fluorescence Spectroscopy. 1991;53-126 Plenum Publishing Corporation, New York.
7. Eftink M. R., Wasylenwski Z. Pressure dependence of fluorescence quenching reactions in proteins. Biophys. Chem. 32:1988;121-130.
8. Frauenfelder H., Alberding N. A., Ansari A., Braunstein D., Cowen B. R., Hong M. K., Iben I. E. T., Johnson J. B., Luck S., Marde M. C., Mourant J. R., Ormos P., Reinisch L., Scholl R., Schulte A. et al. Proteins and pressure. J. Phys. Chem. 94:1990;1024-1037.
9. 562examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry. 37:1998;9877-9883.
10. Gekko K., Hasegawa Y. Compressibility-structure of globular proteins. Biochemistry. 25:1986;6563-6571.
11. Gonnelli M., Strambini G. B. Phosphorescence lifetime of tryptophan in proteins. Biochemistry. 34:1995;13847-13857.
12. Gross M., Auerbach G., Jaenicke R. The catalytic activities of monomeric enzymes show complex pressure dependence. FEBS Letters. 321:1993;256-260.
13. Heremans K., Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta. 1386:1998;353-370.
14. Hitchens K. T., Bryant R. G. Pressure dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 Lysozyme. Biochemistry. 37:1998;5878-5887.
15. Hummer G., Garde S., Garcia A. E., Paulatis M. E., Pratt L. R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl Acad. Sci. USA. 95:1998;1552-1555.
16. Jaenicke R. Enzymes under extremes of physical conditions. Annu. Rev. Biophys.Bioeng. 10:1981;1-67.
17. Jonas J., Ballard L., Nash D. High-resolution, high-pressure NMR studies of proteins. Biophys. J. 75:1998;445-452.
18. Lange R., Heiber-Langer I., Bonfils C., Fabre I., Negishi M., Balny C. Activation volume and energetic properties of the binding of CO to hemoproteins. Biophys. J. 66:1994;89-98.
19. Low P. S., Somero G. N. Activation volumes in enzymatic catalysis: their sources and modification by low-molecular-weight solutes. Proc. Natl Acad. Sci. USA. 72:1975;3014-3018.
20. Oliveira A. C., Gaspar L. P., Da Poian A. T., Silva J. Arc repressor will not denature under pressure in the absence of water. J. Mol. Biol. 240:1994;184-187.
21. Privalov P., Makhatadze G. I. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J. Mol. Biol. 232:1993;660-679.
22. Silva J. L., Weber G. Pressure stability of proteins. Annu. Rev. Phys. Chem. 44:1993;89-113.
23. Silva J. L., Luan P., Glaser M., Voss E. W., Weber G. Effects of hydrostatic pressure on a membrane-enveloped virus: high immunogenecity of the pressure-inactivated virus. J. Virol. 66:1992;2111-2117.
24. Strambini G. B., Gonnelli M. Tryptophan phosphorescence in fluid solution. J. Am. Chem. Soc. 117:1995;7646-7651.
25. Tang K. E. S., Dill K. A. Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability. J. Biomol. Struct. Dynam. 16:1998;397-411.
26. Vanderkooi J. M. Tryptophan phosphorescence from proteins at room temperature. Lakowicz J. R. Topics in Fluorescence Spectroscopy. 1991;113-136 Plenum Publishing Corporation, New York.
27. Vanderkooi J. M., Englander S. W., Papp S., Wright W. W., Owen C. S. Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence. Proc. Natl Acad. Sci. USA. 87:1990;5099-5103.
28. Vidugiris G. J., Markley J. L., Royer C. Evidence for a molten globule-like transition state in protein floding from determination of activation volumes. Biochemistry. 34:1995;4909-4912.
29. Wagner G. Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. Quart. Rev. Biophys. 16:1983;1-57.
30. Weber G. Dissociation of oligomeric proteins by hydrostatic pressure. Van Eldyk R., Jonas J. High Pressure Chemistry and Biochemistry. 1987;401-420 NATO ASI Series. Math. Phys. Sci. Dordrecht.
31. Wuthrich K., Wagner G., Richarz R., Baum W. Correlations between internal mobility and stability of globular proteins. Biophys. J. 32:1980;549-560.
32. Zavodsky P., Kardos J., Svingor A., Petsko G. A. Adjustment of conformational flexibility is a key event in the thermal adaptations of proteins. Proc. Natl Acad. Sci. USA. 95:1998;7406-7411.
33. Zipp A., Kauzmann W. Pressure denaturation of metmyoblobin. Biochemistry. 12:1973;4217-4228.