Identification and characterization of molten globule-like state of hen egg-white lysozyme in presence of salts under alkaline conditions

Protein and Peptide Letters

Volumn 17, Issue 1, 2010, Pages 11-17

  Ansari, M A ^a   Zubair, S ^a   Atif, S M ^a   Kashif, M ^a   Khan, N ^a   Rehan, M ^a   Anwar, T ^a   Iqbal, A ^a   Owais, M ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Lysozyme; Molten globule; Secondary structure

Indexed keywords

ACRYLAMIDE; INORGANIC SALT; LYSOZYME; POTASSIUM CHLORIDE; TRYPTOPHAN;

ANIMAL; ARTICLE; CHEMISTRY; CHICKEN; CIRCULAR DICHROISM; METABOLISM; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROFLUOROMETRY;

ACRYLAMIDE; ANIMALS; CHICKENS; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN-ION CONCENTRATION; MURAMIDASE; POTASSIUM CHLORIDE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SALTS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 77949990336     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986610789909502     Document Type: Article

References (59)

1. Wada, A.; Nakamura, H. Nature of the charge distribution in proteins. Nature, 1981, 293(5835), 757-758.
2. Perry, K.M.; Onuffer, J.J.; Gittleman, M.S.; Baramet, L.; Matthews, C.R. Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Bio-chemistry, 1989, 28(19), 7961-7968.
3. Spector, S.; Wang, M.; Carp, S.A.; Robblee, J.; Hendsch, Z. S.; Fairman, R.; Tidor, B. Raleigh, D. P. Rational modification of protein stability by the mutation of charged surface residues. Biochemistry, 2000, 39(5), 872-879.
4. Loladze, V.V.; Ibarra-Molero, B.; Sanchez-Ruiz, J.M.; Makhatadze, G.I. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry, 1999, 38(50), 16419-16423.
5. Pace, C.N.; Grimsely, G.R. Ribonuclease T1 is stabilized by cation and anion binding. Biochemistry, 1988, 27(9), 3242-3246.
6. Schulz, H. On the structure-function relationship of acyl carrier protein of Escherichia coli. J. Biol. Chem., 1975, 250(7), 2299-2304.
7. Von Hippel, P.H.; Schleich, T. In Structure and stability of biological macromolecules, Timasheff, S.N.; Fasman, G.D. Eds.; Marcel Dekker Inc: New York, 1969, Vol. 2, pp. 417-574.
8. Arakawa, T.; Bhat, R.; Timasheff, S. N. Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system. Biochemistry, 1990, 29(7), 1924-1931.
9. Schellman, J.A. Selective binding and solvent denaturation. Biopolymers, 1987, 26(4), 549-559.
10. Timasheff, S.N. Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. Biochemistry, 1992, 31(41), 9857-9864.
11. Timasheff, S.N. Solvent stabilization of protein structure. Methods Mol. Biol., 1995, 40, 253-269.
12. Gilson, M.K. Theory of electrostatic interactions in macromolecules. Curr. Opin. Struct. Biol., (1995), 5(2), 216-223.
13. Jackson, S.E; Fersht, A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry, 1991, 30(43), 10428-10435.
14. De Prat Gay, G.; Ruiz-Sanz, J.; Neira, J.L.; Itzhaki, L.S.; Fersht, A.R. Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module. Proc. Natl. Acad. Sci. USA, 1995, 92(9), 3683-3686.
15. Kragelund, B.B.; Robinson, C.V.; Knudsen, J.; Dobson, C.M.; Poulsen, F.M. Folding of a four-helix bundle: studies of acylcoenzyme A binding protein. Biochemistry, 1995, 34(21), 7217-7224.
16. Schindler, T.; Herrler, M.; Marahiel, M.A.; Schmid, F.X. Extremely rapid protein folding in the absence of intermediates. Nature Struc. Biol., 1995, 2(8), 663-673.
17. Miranker, A.D.; Dobson, C.M. Collapse and co-operativity in protein folding. Curr. Opin. Struc. Biol., 1996, 6(1), 31-42.
18. Chaffotte, A.F.; Guillou, Y. M.; Goldberg, E. Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry, 1992, 31(40), 9694-9702.
19. Radford, S.E.; Dobson, C.M.; Evans, P.A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature, 1992, 358(6384), 302-307.
20. Dobson, C.M.; Evans, P.A.; Radford, S.E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci., 1994, 19(1), 31-37.
21. Eyles, S.J.; Radford, S.E.; Dobson, C.M. Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme. Biochemistry, 1994, 33(44), 13038-13048.
22. Hooke, S.D.; Radford, S.E.; Dobson, C.M. The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme. Biochemistry, 1994, 33(19), 5867-5876.
23. Matagne, A.; Radford, S.E.; Dobson, C.M. Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process. J. Mol. Biol., 1997, 267(5), 1068-1074.
24. Artymiuk, P.J.; Blake, C.C. Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions. J. Mol. Biol., 1981, 152(5), 737-762.
25. Kiefhaber, T. Kinetic traps in lysozyme folding. Proc. Natl. Acad. Sci. USA, 1995, 92(20), 9029-9033.
26. Rothwarf, D.M.; Scheraga, H.A. Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry, 1996, 35(43), 13797-13807.
27. Lu, H.; Buck, M.; Radford, S.E.; Dobson, C.M. Acceleration of the folding of hen lysozyme by trifluoroethanol. J. Mol. Biol., 1997, 265(2), 112-117.
28. Von den Berg, B.; Chung, E.W.; Robinson, C.V.; Mateo, P.L.; Dobson, C.M. The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase. EMBO J., 1999, 18(17), 4794-4803.
29. Lowry, O.H.; Rosebrough, N.; Farr, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem., 1951, 193(1), 265-275.
30. Khurana, R.; Udgaonkar, J.B. Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule. Biochemistry, 1994, 33(1), 106-115.
31. Chen, Y.H.; Yang, J.T.; Martinez, H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry, 1972, 11(22), 4120-4131.
32. Pazur, J.H.; Kleppe, K.; Cepure, A. A glycoprotein structure for glucose oxidase from Aspergillus niger. Arch. Biochem. Biophys., 1965, 111(2), 3517-3527.
33. Kim, P.S.; Baldwin, R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem., 1990, 59, 631-660.
34. Matthews, C.R. Pathways of protein folding. Annu. Rev. Biochem., 1993, 62, 653-683.
35. Plaxco, K.W.; Dobson, C.M. Time-resolved biophysical methods in the study of protein folding. Curr. Opin. Struc. Biol., 1996, 6(5), 630-636.
36. Dobson, C.M. Finding the right fold. Nature Struc. Biol., 1995, 2(7), 513-517.
37. Baldwin, R.L. The nature of protein folding pathways: The classical versus the new view. J. Biomolecular NMR, 1995, 5(2), 103-109.
38. Redfield, C.; Smith R.A.G.; Dobson, C.M. Structural characterization of a highly-ordered ' molten globule' at. low pH. Nat. Struc. Biol., 1994, 1(1), 23-28
39. Nolting, B.; Golbik, R.; Fersht, A. R. Submillisecond events in protein folding. Proc Natl. Acad. Sci. USA, 1995, 92(23), 10668-10672.
40. Plaxco, K.W.; Dobson, C.M. Time-resolved biophysical methods in the study of protein folding. Curr. Opin. Struc. Biol., 1996, 6(5), 630-636.
41. Ptitsyn, O.B. Kinetic and equilibrium intermediates in protein folding. Protein Eng., 1994, 7(5), 593-596.
42. Radford, S.E.; Dobson, C.M. Insights into protein folding using physical techniques: studies of lysozyme and alpha-lactalbumin. Phil. Trans. R. Soc. Lond. B Biol. Sci., 1995, 348(1323), 17-25.
43. Privalov, P.L. Intermediate states in protein folding. J. Mol. Biol., 1996, 258(5), 707-725.
44. Arai, M.; Kuwajima, K. Role of the molten globule state in protein folding. Adv. Protein Chem., 2000, 53, 209-282.
45. Das, B.K.; Bhattacharyya, T.; Roy, S. Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli. Biochemistry, 1995, 34(15), 5242-5247.
46. Ogasahara, K.; Matsushita, E.; Yatuni, K. Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule. J. Mol. Biol., 1993, 234(4), 1197-1206.
47. Jeng, M.F.; Englander, S.W. Stable submolecular folding units in a non-compact form of cytochrome C. J. Mol. Biol., 1991, 221(3), 1045-1061.
48. Goto, Y.; Takahashi, N.; Fink, A.L. Mechanism of acid-induced folding of proteins. Biochemistry, 1990, 29(14), 3480-3488.
49. Ali, V.; Prakash, K.; Kulkarni, S.; Ahmad, A.; Madhusudan, K.P.; Bhakuni, V. 8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions. Biochemistry, 1999, 38(41), 13635-13642.
50. 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, 1991, 31(1), 119-128.
51. Kuwajima, K.; Hiraoka, Y.; Ikeguchi, M.; Sugai, S. Comparison of the transient folding intermediates in lysozyme and alphalactalbumin. Biochemistry, 1985, 24(4), 874-881.
52. Buck, M.; Radford, S.E.; Dobson, C.M. A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. Biochemistry, 1993, 32(2), 669-678.
53. Venyaminov, S.Yu.; Yang, J.T. In Circular Dichroism and the Conformational analysis of biomolecules, Fasman, G.D., Ed.; Plenum Press: New York, 1996, pp. 69-104.
54. Pawar, S.A.; Deshpande, V.V. Characterization of acid-induced unfolding intermediates of glucose/xylose isomerase. Eur. J. Biochem., 2000, 267(21), 6331-6338.
55. Collins, K.D.; Washabaugh, M.W. The Hofmeister effect and the behaviour of water at interfaces. Q. Rev. Biophys., 1985, 18(4), 323-422.
56. Arakawa, T.; Timasheff, S.N. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry, 1982, 21(25), 6545-6552.
57. Lee, J.C.; Timasheff, S.N. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry, 1974, 13(2), 257-265.
58. Shire, S.J. In Characterization, and Stability of Protein Drugs. Pearlman, R.; Wang, Y.J. Eds. Formulation, Plenum Press: New York, 1996, Vol. 9, pp. 393-426.
59. Kuwajima, K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct. Funct. Genet., 1989, 6(2), 87-103.