Structural differences of ovalbumin and S-ovalbumin revealed by denaturing conditions

Zeitschrift fur Naturforschung Section C - Journal of Biosciences

Volumn 52, Issue 9-10, 1997, Pages 645-653

  Paolinelli, Corrado ^a   Barteri, Mario ^b   Boffi, Federico ^a   Forastieri, Francesca ^a   Gaudiano, Maria Cristina ^b   Della Longa, Stefano ^c   Castellano, Agostina Congiu ^a  

^a UNIVERSITÀ DI ROMA LA SAPIENZA   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c UNIVERSITY OF L'AQUILA   (Italy)

Author keywords

Circular Dichroism; Conformational Changes; Protein Folding; Protein Structure; Synchrotron Radiation; X Ray Scattering

Indexed keywords

EID: 0031238975     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1997-9-1012     Document Type: Article

References (39)

1. Abrego J. R. B., Craievich A. F., Mascarenhas Y. P. and Laure C. J. (1993), SAXS study of crotapotin at low pH. Biophys. J. 64, 560-564.
2. Batra P. P., Sasa K., Ueki T. and Takeda K. (1989), Circular dichroic study of conformational changes in ovalbumin induced by modification of sulfhydryl groups and disulfide reduction. J. Protein Chem. 8, 609-617.
3. Batra P. P., Sasa K., Ueki T. and Takeda K. (1989), Circular dichroic study of conformational changes in ovalbumin. J. Protein Chem. 8, 221-229.
4. Chan H. S. and Dill K. A. (1989), Compact polymers. Macromolecules 22, 4559-4573.
5. Congiu Castellano A., Barteri M., Bianconi A., Della Longa S. and Paolinelli C. (1996), Conformational changes involved in the switch from ovalbumin to S-ovalbumin. Z. Naturforsch. 51 c , 379-385.
6. Dill K. A. and Shortle D. (1991), Denatured states of proteins. Annu. Rev. Biochem. 60, 795-825.
7. Donovan J. W. and Mapes C. J. (1976), A differential scanning calorimetric study of conversion of ovalbumin to S-ovalbumin in Eggs. J. Sci. Food Agric. 27, 197-204.
8. Durchschlag H., Zipper P., Wilfing R. and Purr G. (1991), Detection of small conformational changes of proteins by small-angle scattering. J. Appl. Cryst. 24, 822-831.
9. Egelandsdal B. (1986), Conformation and structure of mildly heat-treated ovalbumin in dilute solutions and gel formation at higher protein concentrations. Int. J. Peptide Protein Res. 28, 560-568.
10. Fontana A., Nardone M. and Ricci M. A. (1995), Depolarized Rayleigh scattering in water up to supercritical conditions. J. Chem. Phys. 102, 6975-6981.
11. Fothergill L. A. and Fothergill J. E. (1970), Thiol and disulphide contents of hen ovalbumin. Biochem. J. 116, 555-561.
12. Garrigos M., Mallam S., Vachette P. and Bordas J. (1992), Structure of the myosin head in solution and the effect of light chain 2 removal. Biophys. J. 63, 1462-1470.
13. Glazer A. N., McKenzie H. A. and Wake R. G. (1963), The denaturation of Proteins. II Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution. Biochim. Biophys. Acta 69, 240-248.
14. Gorbunoff M. J. (1969), Exposure of tyrosine residues in proteins. III The reaction of cyanuric fluoride and N-Acetylimidazole with ovalbumin, chymotrypsinogen, and trypsinogen. Biochemistry 8, 2591-2598.
15. Gorinstein S., Zemser M., Friedman M. and Chang SH.-M. (1995), Simultaneous differential scanning calorimetry, X-ray diffraction and FTIR spectrometry in studies of ovalbumin denaturation. Int. J. Peptide Protein. Res. 45, 248-256.
16. Guinier A. and Fournet G. (1955), Small angle scattering of X-rays. John Wiley & Sons, Inc, New York.
17. 31P NMR and water proton relaxation rate enhancements. Biochemistry 25, 84-94.
18. Honeycutt J. D. and Thirumalai D. (1992), The nature of folded states of globular proteins. Biopolymers 32, 695-709.
19. Kint S. and Tomimatsu Y. (1979), Raman difference spectroscopic investigation of ovalbumin and S-ovalbumin. Biopolymers 18, 1073-1079.
20. Koseki T., Kitabatake N. and Doi E. F. (1988), Conformational chances in ovalbumin at acid pH. Biochem. J. 103, 425-430.
21. Matsumoto T. and Chiba J. (1990), Rheological and small-angle X-ray scattering investigations on the shape and ordered arrangement of native ovalbumin molecules in acqueous colloids. J. Chem. Soc. Faraday Trans. 86, 2877-2882.
22. Myers J. K., Pace C. N. and Scholtz J. M. (1995), Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Science 4, 2138-2148.
23. Nakamura R., Hirai M. and Takemori Y. (1980), Some differences noted between the properties of ovalbumin and S-ovalbumin in native state. Agric. Biol. Chem. 44, 149-153.
24. Nakamura R., Takemori Y. and Shitamori S (1981), Liberation of carboxyl groups on conversion of ovalbumin to S-ovalbumin. Agric. Biol. Chem. 45, 1653-1659.
25. Nakamura R. and Ishimaru M. (1981), Changes in the shape and surface hydrophobicity of ovalbumin during its transformation to S-ovalbumin. Agric. Biol. Chem. 45, 2775-2780.
26. Nisbet A. D., Saundry R. M., Moir A. J. G., Fothergill L. A. and Fothergill J. E. (1981), The complete amino-acid sequence of hen ovalbumin. Eur. J. Biochem. 115, 335-345.
27. Pace C. N. (1975), The stability of globular proteins. CRC Crit. Rev. Biochem. 3, 1-43.
28. Painter P. C. and Koenig J. L. (1976), Raman spectroscopy study of the proteins of egg white. Biopolymers 15, 2155-2166.
29. Smith M. B. (1964), Studies on ovalbumin I. Denaturation by heat and the heterogeneity of ovalbumin. Aust. J. Biol. Sci. 17, 261-270.
30. Smith M. B. and Back J. F. (1965), Studies on ovalbumin II. The formation and properties of S-ovalbumin, a more stable form of ovalbumin. Aust. J. Biol. Sci. 18, 365-77.
31. Smith M. B. and Back J. F. (1968a), Studies on ovalbumin III. Denaturation of ovalbumin and S-ovalhumin. Aust. J. Biol. Sci. 21, 539-48.
32. Smith M. B. and Back J. F. (1968b), Studies on ovalbumin IV. Trypsin digestion and the cystine peptides of ovalbumin and S-ovalbumin. Aust. J. Biol. Sci. 21, 549-58.
33. Stein P. E., Leslie A. G. W., Finch J. T. and Carrell R. W. (1991), Crystal structure of uncleaved ovalbumin at 1.95 Å resolution. J. Mol. Biol. 221, 941-959.
34. Taborsky G. (1974), Phosphoproteins. Adv. Protein Chem. 28, 1-210.
35. Takeda K. and Moriyama Y. (1990), Circular dichroism studies on helical structure preferences of amino acid residues of proteins caused by sodium dodecyl sulfate. J. Protein Chem. 9, 573-582.
36. Takeda K., Shigemura A., Hamada S., Gu W., Fang D., Sasa K. and Hachiya K. (1992), Dependance of reaction rate of 5,5′-dithiobis-(2-nitrobenzoic acid) to free sulfhydryl groups of bovine serum albumin and ovalbumin on the protein conformations. J. Protein Chem. 11, 187-192.
37. Tanford C. (1968), Protein denaturation. Adv. Protein Chem. 23, 121-282.
38. Williams R. W. (1986), Protein secondary structure analysis using Raman amide I and amide III spectra. Methods Enzymol. 130, 311-338.
39. Zemser M., Friedman M., Katzhendler J., Greene L. L., Minsky A. and Gorinstein S. (1994), Relationship between functional properties and structure of ovalbumin. J. Protein Chem. 13, 261-274.