Molten globule-like state of human serum albumin at low ph

European Journal of Biochemistry

Volumn 266, Issue 1, 1999, Pages 26-32

  Muzammil, Salman ^b   Kumar, Yogesh ^b   Tayyab, Saad ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

^b NONE

Author keywords

Acid denaturation; Human serum albumin (HSA); Molten globule; PH

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLAMIDE; GUANIDINE; HUMAN SERUM ALBUMIN; TRYPTOPHAN;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; HUMAN; ISOMERISM; MATHEMATICAL COMPUTING; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; TEMPERATURE DEPENDENCE; VISCOSITY;

ANILINO NAPHTHALENESULFONATES; CIRCULAR DICHROISM; HEAT; HUMANS; HYDROGEN-ION CONCENTRATION; ISOMERISM; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SERUM ALBUMIN; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; VISCOSITY;

EID: 0002829561     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00810.x     Document Type: Article

References (43)

1. 1. Wetlaufer, D.B. (1973) Nucleation, rapid folding and globular intrachain regions in proteins. Proc. Natl Acad. Sci. USA 70, 697-701.
2. 2. Anson, M.L. (1945) Protein denaturation and the properties of protein groups. Adv. Protein Chem. 2, 361-386.
3. 3. Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science 181, 223-230.
4. 4. Dill, K.A. & Shortle, D. (1991) Denatured states of proteins. Annu. Rev. Biochem. 60, 795-825.
5. 5. Schellman, J.A. (1994) The thermodynamics of solvent exchange. Biopolymers 34, 1015-1026.
6. 6. Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular proteins. Proteins 6, 87-103.
7. 7. Yu, X.-C., Shen, S. & Strobel, H.W. (1995) Denaturation of cytochrome P450 2B1 by guanidine hydrochloride and urea: evidence for a metastable intermediate state of the active site. Biochemistry 34, 5511-5517.
8. 8. Ptitsyn, O.B. (1995) Molten globule and protein folding. Adv. Protein Chem. 47, 83-229.
9. 9. Filippis, D.E., Vassiliev, V.B., Beltramin, M., Fontana, A., Salvato, B. & Gaitskhoki, V.S. (1996) Evidence for the molten globule state of human apo-ceruloplasmin. Biochim. Biophys. Acta 1297, 119-123.
10. 10. Tanford, C. (1968) Protein denaturation (parts A & B). Adv. Protein Chem. 23, 121-282.
11. 11. Dobson, C.M. (1992) Unfolded proteins, compact states and molten globules. Curr. Opin. Struc. Biol. 2, 6-12.
12. 12. Ptitsyn, O.B. (1992) Protein Folding (Creighton, T.E., ed.), pp. 243-300. W. H. Freeman, New York.
13. 13. Aune, K.C., Salahuddin, A., Zarlengo, M.H. & Tanford, C. (1967) Evidence for residual structure in acid and heat denatured proteins. J. Biol. Chem. 242, 4486-4489.
14. 14. Tanford, C. (1970) Protein denaturation (part C). Adv. Protein Chem. 24, 1-95.
15. 15. Fink, A.L., Calciano, L.J., Goto, Y., Kurotsu, T. & Palleros, D.R. (1994) Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33, 12504-12511.
16. 16. Goto, Y., Takahashi, N. & Fink, A.L. (1990) Mechanism of acid-induced folding of proteins. Biochemistry 29, 3480-3488.
17. 17. Buchner, J., Renner, M., Lilie, H., Hinz, H., Jaenicke, R., Kiefhaber, T. & Rudolph, R. (1991) Alternatively folded states of an immunoglobulin. Biochemistry 30, 6922-6929.
18. 18. Carra, J.H., Elizabeth, A.A. & Privalov, P.L. (1994) Thermodynamics of staphylococcal nuclease denaturation. I. The acid denatured state. Protein Sci. 3, 944-951.
19. 19. Dobson, C.M. (1994) Solid evidence for molten globule. Curr. Biol. 4, 636-640.
20. 20. Bycroft, M., Matouschek, A., Kellis, J.T. Jr, Serrano, L. & Fersht, A.R. (1990) Detection and characterization of a folding intermediate in barnase by NMR. Nature (London) 346, 488-490.
21. 21. Serrano, L., Matouschek, A. & Fersht, A.R. (1992) The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224, 805-818.
22. 2O. Biochemistry 32, 11878-11885.
23. 23. Tanford, C., Buzzell, J.G., Rands, D.G. & Swanson, S.A. (1955) The reversible acid expansion of bovine serum albumin. J. Am. Chem. Soc. 77, 6421-6428.
24. 24. Foster, J.F. (1960) The Plasma Proteins (Putnam, F.W., ed.), Vol. 1, pp. 179-239. Academic Press, New York.
25. 25. Peters, T. Jr (1985) Serum albumin. Adv. Protein Chem. 37, 161-245.
26. 26. Sadler, P.J. & Tucker, A. (1993) pH-induced structural transitions of bovine serum albumin: histidine pKa values and unfolding of the N-terminus during the N to F transition. Eur. J. Biochem. 212, 811-817.
27. 27. Wallevik, K. (1973) Reversible denaturation of human serum albumin by pH, temperature and guanidine hydrochloride. J. Biol. Chem. 245, 2650-2655.
28. 28. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the Folin-phenol reagent. J. Biol. Chem. 193, 265-275.
29. 29. Mulqueen, P.M. & Kronman, M.J. (1982) Binding of naphthalene dye to the N and A conformers of bovine α-lactalbumin. Arch. Biochem. Biophys. 215, 28-39.
30. 30. Chen, Y.-H., Yang, J.T. & Martinez, H. (1972) Determination of the secondary structure of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131.
31. 31. Eftink, M.R. & Ghiron, C.A. (1982) Fluorescence quenching studies with proteins. Anal. Biochem. 114, 199-227.
32. 32. Ahmad, F. & Salahuddin, A. (1974) Influence of temperature on the intrinsic viscosities of proteins in random coil conformation. Biochemistry 13, 245-249.
33. 33. Johnson, C.M. & Fersht, A.R. (1995) Protein stability as a function of denaturant concentration: thermal stability of barnase in the presence of urea. Biochemistry 34, 6795-6808.
34. 34. Stryer, L. (1965) The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of nonpolar binding site. J. Mol. Biol. 13, 482-495.
35. 35. Lee, J.Y. & Hirose, M. (1992) Partially folded state of disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation. J. Biol. Chem. 267, 14753-14758.
36. 36. He, X.M. & Carter, D.C. (1992) Atomic structure and chemistry of human serum albumin. Nature (London) 358, 209-215.
37. 37. Reed, R.G., Feldhoff, R.C., Clute, O.L. & Peters, T. Jr (1975). Fragments of bovine serum albumin produced by limited proteolysis. Conformation and ligand binding. Biochemistry 14, 4578-4583.
38. 38. Engelhard, M. & Evans, P.A. (1995) 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, 1553-1562.
39. 39. Peng, Z.-Y. & Kim, P.S. (1994) A protein dissection study of a molten globule. Biochemistry 33, 2136-2141.
40. 40. Reddi, E., Lambert, C.R., Jori, G. & Rodgers, M.A. (1987) Photokinetic and photophysical measurements of the sensitized photooxidation of the tryptophyl residue in N-acetyltryptophanamide and in human serum albumin. Photochem. Photobiol. 45, 345-351.
41. 41. Peterman, B.F. & Laidler, K.J. (1980) Study of reactivity of tryptophan residues in serum albumin and lysozyme by N-bromosuccinimide fluorescence quenching. Arch. Biochem. Biophys. 199, 158-164.
42. 42. Bychkova, V.E., Berni, R., Rossi, G.L., Kutyshenko, V.P. & Ptitsyn, O.B. (1992) Retinol binding protein is in the molten globule state at low pH. Biochemistry 31, 7566-7571.
43. 43. Khan, M.Y. (1986) Direct evidence for the involvement of the domain III in the N-F transition of bovine serum albumin. Biochem. J. 236, 307-310.