Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS)

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1385, Issue 1, 1998, Pages 69-77

  Sirangelo, Ivana ^a   Bismuto, Ettore ^a   Tavassi, Simona ^a   Irace, Gaetano ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

Author keywords

ANS apomyoglobin complex; ANS apomyoglobin, fluorescence; ANS apomyoglobin, fluorescence decay; Apomyoglobin intermediate

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; APOPROTEIN; FLUORESCENT DYE; MYOGLOBIN;

ABSORPTION SPECTROSCOPY; ARTICLE; FLUORESCENCE; FLUOROMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

ANILINO NAPHTHALENESULFONATES; ANIMALS; APOPROTEINS; BINDING SITES; FLUORESCENT DYES; HORSES; HYDROGEN-ION CONCENTRATION; MYOGLOBIN; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SOLVENTS; SPECTROMETRY, FLUORESCENCE;

EID: 0031832906     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00038-7     Document Type: Article

References (50)

1. Ptitsyn O.B. Protein folding: hypothesis and experiments. J. Protein Chem. 6:1987;273-293.
2. T.E Creighton, Protein: Structure and Molecular Principles, Freeman, New York, 1983.
3. Ogushi M., Wada A. Molten globule state: a compact form of globular proteins with mobile side-chains. FEBS Lett. 164:1983;21-24.
4. Kuwajma K. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins Struct. Func. Genet. 6:1989;87-103.
5. Ptitsyn O.B., Uversky V.N. The molten globule is a third thermodynamic state of protein molecules. FEBS Lett. 341:1994;15-18.
6. Balestrieri C., Colonna G., Giovane A., Irace G., Servillo L. Equilibrium evidence of non-single step transition during guanidine unfolding of apomyoglobins. FEBS Lett. 66:1976;60-64.
7. Irace G., Balestrieri C., Parlato G., Servillo L., Colonna G. Tryptophanyl fluorescence heterogeneity of apomyoglobins. Correlations with the presence of two distinct structural domains. Biochemistry. 20:1981;792-799.
8. Bismuto E., Colonna G., Irace G. Unfolding pathway of myoglobin. Evidence for a multistate process. Biochemistry. 22:1983;4165-4170.
9. Irace G., Bismuto E., Savy F., Colonna G. Unfolding pathway of myoglobin: molecular properties of intermediate forms. Arch. Biochem. Biophys. 244(2):1986;459-469.
10. Griko Y.V., Privalov P.L., Venyaminov S.Y., Kutyshenko V.P. Thermodynamic study of the apomyoglobin structure. J. Mol. Biol. 202:1988;127-138.
11. Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548.
12. Barrick D., Baldwin R.L. Three state analysis of sperm whale apomyoglobin folding. Biochemistry. 32:1993;3790-3796.
13. Barrick D., Baldwin R.L. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2:1993;869-876.
14. Barrick D., Hughson F.M., Baldwin R.L. Molecular mechanism of acid denaturation. The role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol. 237:1994;588-601.
15. Griko Y.V., Privalov P.L. Thermodynamic puzzle of apomyoglobin unfolding. J. Mol. Biol. 235:1994;1318-1325.
16. Eliezer D., Jennings P.A., Wright P.E., Doniacus S., Hodgson K.O., Tsuruta H. The radius of gyration of an apomyoglobin folding intermediate. Science. 270:1995;487-488.
17. Hughson F.M., Baldwin R.L. Use of site directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry. 28:1989;4415-4422.
18. Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896.
19. Loh S.N., Kay M.S., Baldwin R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. U.S.A. 92(12):1995;5446-5450.
20. De Sanctis G., Ascoli F., Brunori M. Folding of apominimyoglobin. Proc. Natl. Acad. Sci. U.S.A. 91:1994;11507-11511.
21. Semisotnov G.V., Rodionova N.A., Razgulyaev O.I., Uversky V.N., Gripas A.F., Gilmanshin R.I. Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 31:1991;119-128.
22. Bismuto E., Gratton E., Sirangelo I., Irace G. Structure and dynamics of the acidic compact state of apomyoglobin by frequency-domain fluorometry. Eur. J. Biochem. 218:1993;213-219.
23. Bismuto E., Irace G., Sirangelo I., Gratton E. Pressure induced perturbation of ANS-apomyoglobin complex: frequency domain fluorescence studies on native and acidic compact states. Protein Sci. 5:1996;121-126.
24. Bismuto E., Sirangelo I., Irace G., Gratton E. Pressure induced perturbation of apomyoglobin structure: fluorescence studies on native and acidic compact forms. Biochemistry. 35:1996;1173-1178.
25. Sirangelo I., Bismuto E., Irace G. Solvent denaturation of the acidic compact state of apomyoglobin. FEBS Lett. 338:1994;11-15.
26. Teale F.W.J. Cleavage of heme-protein link by acid methylethylketone. Biochim. Biophys. Acta. 35:1959;543.
27. Colonna G., Irace G., Bismuto E., Servillo L., Balestrieri C. Structural and functional aspects of the heart ventricle myoglobin of bluefin tuna. Comp. Biochem. Physiol. 76A:1983;481-485.
28. Wetlaufer D.B. Ultraviolet spectra of proteins and amino acid. Adv. Protein Chem. 17:1962;303-390.
29. Weber G., Young L.B. Fragmentation of bovine serum albumin by pepsin. J. Biol. Chem. 239:1964;1415-1423.
30. Ragone R., Colonna G., Balestrieri C., Servillo L., Irace G. Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry. 23:1984;1871-1875.
31. Gratton E., Limkeman M., Lakowicz J.R., Maliwal B., Cherek H., Laczko G. Resolution of mixtures of fluorophores using phase and modulation data. Biophys. J. 46:1984;479-486.
32. Lakowicz J.R., Laczko G., Cherek H., Gratton E., Limkeman M. Analysis of the fluorescence decay kinetics from variable-frequency phase shift and modulation data. Biophys. J. 46:1984;463-471.
33. Alcalà R., Gratton E., Prendergast D.M. Fluorescence lifetime distributions in proteins by use of multifrequency phase fluorometry. Biophys. J. 51:1987;925-936.
34. Beechem J. Global analysis of biochemical and biophysical data. Meth. Enzymol. 210:1992;37-54.
35. Stryer L. The interaction of a naphthalene sulfonate dye with apomyoglobin and apohemoglobin: a fluorescence probe of non polar binding site. J. Mol. Biol. 13:1965;482-495.
36. Breslow E., Koheler R., Girotti A.W. Properties of protoporphyrin-apomyoglobin complexes and related compounds. J. Biol. Chem. 242:1967;4149-4156.
37. Cocco M.J., Lecomte T.J.J. The native state of apomyoglobin described by proton NMR spectroscopy: interaction with paramagnetic probe HyTEMPO and the fluorescent dye ANS. Protein Sci. 3:1994;267-271.
38. Colonna G., Balestrieri C., Bismuto E., Servillo L., Irace G. Heme and cysteine microenvironments of tuna apomyoglobin. Evidence of two independent unfolding regions. Biochemistry. 21:1982;212-215.
39. Hargrove M.S., Olson J.S. The stability of holomyoglobin is determined by heme affinity. Biochemistry. 35:1996;11310-11318.
40. Cocco M.J., Kao Y.H., Phillips A.T., Lecomte T.J.J. Structural comparison of apomyoglobin and metaquomyoglobin: pH titrations of histidines by NMR spectroscopy. Biochemistry. 31:1992;6481-6491.
41. Kirby E.P., Steiner R.F. The tryptophan microenvironments in apomyoglobin. J. Biol. Chem. 245:1970;6300-6306.
42. Colonna G., Irace G., Parlato G., Aloj S.M., Balestrieri C. The effect of evolution on homologous proteins. A comparison between the chromophore microenvironments of italian water buffalo (Bos bubalus L.) and sperm whale apomyoglobin. Biochem. Biophys. Acta. 532:1978;354-367.
43. Bismuto E., Sirangelo I., Irace G. Salt-induced refolding of myoglobin at acidic pH: molecular properties of a partly folded intermediate. Arch. Biochem. Biophys. 298(2):1992;624-629.
44. Bismuto E., Irace G. Unfolding pathway of apomyoglobin: simultaneous characterization of acidic conformational states by frequency domain fluorometry. J. Mol. Biol. 241:1994;103-109.
45. Goto Y., Fink A.L. Phase diagram for acidic conformational states of apomyoglobin. J. Mol. Biol. 214:1990;803-805.
46. Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249:1995;215-228.
47. Nishii I., Kataoka M., Tokunaga F., Goto Y. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry. 33:1994;4903-4909.
48. Nishii I., Kataoka M., Goto Y. Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250:1995;223-238.
49. Ptitsyn O.B. Structures of folding intermediates. Curr. Opin. Struct. Biol. 5:1995;74-78.
50. Engelhard M., Evans P.A. Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates. Protein Sci. 4:1995;1553-1562.