Guanidinium chloride and urea denaturations of β-Lactoglobulin A at pH 2.0 and 25 °C: The equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches)

Biophysical Chemistry

Volumn 127, Issue 3, 2007, Pages 140-148

  Dar, Tanveer Ali ^a   Singh, Laishram Rajendrakumar ^c   Islam, Asimul ^a   Anjum, Farah ^a   Moosavi Movahedi, Ali Akbar ^b   Ahmad, Faizan ^a  

^a JAMIA MILLIA ISLAMIA CENTRAL UNIVERSITY   (India)

^b UNIVERSITY OF TEHRAN   (Iran)

^c FOX CHASE CANCER CENTER   (United States)

Author keywords

lactoglobulin; Guanidinium chloride denaturation; Non native intermediate; Protein folding; Protein stability; Urea denaturation

Indexed keywords

BETA LACTOGLOBULIN; GUANIDINE; TRYPTOPHAN; UREA;

ARTICLE; CHEMICAL BINDING; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; DENATURATION; EQUILIBRIUM CONSTANT; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; PH; PRIORITY JOURNAL; ULTRAVIOLET RADIATION; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; CATTLE; CIRCULAR DICHROISM; GUANIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOGLOBULINS; PARASYMPATHOMIMETICS; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPTOPHAN; UREA;

BOVINAE;

EID: 33947408769     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.01.006     Document Type: Article

References (49)

1. Gregersen N. Protein misfolding disorders: pathogenesis and intervention. J. Inherit. Metab. Dis. 29 (2006) 456-470
2. Chaudhuri T.K., and Paul S. Protein-misfolding and chaperone-based therapeutic approaches. FEBS J. 273 (2006) 1331-1349
3. Carrell R.W. Cell toxicity and conformational diseases. Trends Cell Biol. 15 (2005) 574-580
4. Anathanarayan V.S., and Ahmad F. Evidence from rotatory measurements for an intermediate state in the guanidine hydrochloride denaturation of β-lactoglobulin. Can. J. Biochem. 55 (1977) 239-243
5. Hamada D., and Goto Y. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. J. Mol. Biol. 269 (1997) 479-487
6. Balbach J., Forge V., Van Nuland N.A.J., Winder S.L., Hore P.J., and Dobson C.M. Following protein folding in real time using NMR spectroscopy. Nature Struct. Biol. 2 (1995) 865-870
7. Fersht A.R. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 10869-10873
8. Baldwin R.L., and Rose G.D. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem. Sci. 24 (1999) 26-33
9. Baldwin R.L., and Rose G.D. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24 (1999) 77-83
10. Kuwata K., Shastry R., Cheng H., Hoshino M., Batt C.A., Goto Y., and Roder H. Structural and kinetic characterization of early folding events in beta-lactoglobulin. Nat. Struct. Biol. 8 (2001) 151-155
11. Jackson G.S., Hosszu L.L.P., Power A., Hill A.F., Kenney J., Saibil H., Craven C.J., Waltho J.P., Clarke A.R., and Collinge J. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 283 (1999) 1935-1937
12. Ananthanarayan V.S., Ahmad F., and Bigelow C.C. The denaturation of beta-lactoglobulin-A at pH 2. Biochim. Biophys. Acta 492 (1977) 194-203
13. Arai M., and Kuwajima K. Role of the molten globule in protein folding. Adv. Protein Chem. 53 (2000) 209-282
14. Pace N.C., and Tanford C. Thermodynamics of the unfolding of beta-lactoglobulin A in aqueous urea solutions between 5 and 55 degrees. Biochemistry 7 (1968) 198-208
15. Ragona L., Confalonieri L., Zetta L., De Kruif K.G., Mammi S., Peggion E., Longhi R., and Molinari H. Equilibrium unfolding CD studies of bovine beta- lactoglobulin and its 14-52 fragment at acidic Ph. Biopolymers 49 (1999) 441-450
16. Monera O.D., Kay C.M., and Hodges R.S. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3 (1994) 1984-1991
17. Mulqueen P.M., and Kronmann M.J. Binding of naphthalene dyes to the N and A conformers of bovine α-lactalbumin. Arch. Biochem. Biophys. 215 (1982) 28-39
18. Ahmad F., and Bigelow C.C. Estimation of the free energy of stabilization of ribonuclease A, lysozyme, α-lactalbumin, and myoglobin. J. Biol. Chem. 257 (1982) 12935-12938
19. Pace C.N. The stability of globular proteins. CRC Crit. Rev. Biochem. 3 (1975) 1-43
20. Uhrinova S., Smith M.H., Jameson G.B., Uhrin D., Sawyer L., and Barlow P.N. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimmer. Biochemistry 39 (2000) 3565-3574
21. Fogolari F., Ragona L., Zetta L., Romagnoli S., De Kruif K.G., and Molinari H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Lett. 436 (1998) 149-154
22. Sakurai K., Oobatake M., and Goto Y. Salt dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3. Protein Sci. 10 (2001) 2325-2335
23. Brownlow S., Cabral J.H.M., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C.T., and Sawyer L. Bovine beta-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure 5 (1997) 481-495
24. 15N chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form. J. Biol. NMR 12 (1998) 89-107
25. Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., and Jameson G.B. Structural basis of the Tanford transition of bovine beta-lactoglobulin. Biochemistry 37 (1998) 14014-14023
26. Collini M., D'Alfonso L., and Baldini G. New insight on β-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Sci. 9 (2000) 1968-1974
27. Chen Y.H., Yang J.T., and Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11 (1972) 4120-4131
28. Timasheff S.N., Susi H., Townend R., Stevens L., Gorbunoff M.J., and Kumosinski T.F. In: Ramachandran G.N. (Ed). Conformation of Biopolymers vol. 1 (1967), Academic Press, New York 173-196
29. Woo S.L., Creamer L.K., and Richardson T. Chemical phosphorylation of bovine beta-lactoglobulin. J. Agric. Food Chem. 30 (1982) 65-70
30. Hillquist Damon A.J., and Kresheck G.C. Influence of surfactants on the conformation of β-lactoglobulin B using circular dichroism. Biopolymers 21 (1982) 895-908
31. Kuwata K., Hoshino M., Era S., Batt C.A., and Goto Y. α ↔ β Transition of β- lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283 (1998) 731-739
32. Kauffmann E., Darnton N.C., Austin R.H., Batt C., and Gerwert K. Lifetimes of intermediates in the beta-sheet to alpha-helix transition of beta-lactoglobulin by using diffusional IR mixer. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 6646-6649
33. D'Alfonso L., Collini M., and Baldini G. Does β-lactoglobulin denaturation occur via an intermediate state?. Biochemistry 41 (2002) 326-333
34. Tanford C. Protein denaturation. Adv. Protein Chem. 23 (1968) 121-282
35. Lapanje S. Random coil behavior of proteins in concentrated urea solutions. Croat. Chem. Acta 41 (1969) 115-124
36. Santoro M.M., and Bolen D.W. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 31 (1992) 4901-4907
37. Schellman J.A. Selective binding and solvent denaturation. Biopolymers 26 (1987) 549-559
38. Ahmad F., Taneja S., Yadav S., and Haque S.E. A new method for testing the functional dependence of unfolding free energy changes on denaturant concentration. J. Biochem. 115 (1994) 322-327
39. Gupta R., and Ahmad F. Protein stability: functional dependence of denaturational Gibbs free energy on urea concentration. Biochemistry 38 (1999) 2471-2479
40. Gupta R., Yadav S., and Ahmad F. Protein stability: urea-induced versus guanidine-induced unfolding of metmyoglobin. Biochemistry 35 (1996) 11925-11930
41. Ahmad F. Free energy changes on denaturation of ribonuclease-A by mixed denaturants. Effects of combination of guanidine hydrochloride and one of the denaturants, LiBr, LiCl and NaBr. J. Biol. Chem. 259 (1984) 4183-4186
42. Galani D., and Apenten R.K.O. Beta-lactoglobulin denaturation by dissociation-coupled unfolding. Food Res. Int. 32 (1999) 93-100
43. Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4 (1995) 2138-2148
44. Ragona L., Fogolari F., Romagnoli S., Zetta L., Maubois J.L., and Molinari H. Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements. J. Mol. Biol. 293 (1999) 953-969
45. Robinson D.R., and Jencks W.P. The effect of compounds of the urea-guanidinium class on the activity coefficient of acetyltetraglycine ethyl ester and related compounds. J. Am. Chem. Soc. 87 (1965) 2462-2470
46. Timasheff S.N. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 41 (2002) 3473-3482
47. Timasheff S.N. Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9721-9726
48. Bolen D.W., and Baskakov I.V. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310 (2001) 955-963
49. Griko Y.V., and Privalov P.L. Calorimetric study of the heat and cold denaturation of β-lactoglobulin. Biochemistry 31 (1992) 8810-8815