Thermal, chemical and chemothermal denaturation of yeast enolase

Spectroscopy

Volumn 17, Issue 2-3, 2003, Pages 453-467

  Huang, Ping ^a,b   Dong, Aichun ^a  

^a UNIVERSITY OF NORTHERN COLORADO   (United States)

^b QLT Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CONFORMATIONS; ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; THERMAL EFFECTS;

CHEMOTHERMAL DENATURATION;

YEAST;

ENOLASE; FUNGAL ENZYME; GUANIDINE;

CONFERENCE PAPER; ENZYME ACTIVITY; FOURIER TRANSFORMATION; INFRARED SPECTROSCOPY; NONHUMAN; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROSCOPY; TEMPERATURE; THERMAL ANALYSIS; YEAST;

EID: 0037882025     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2003/941801     Document Type: Conference Paper

References (57)

1. J.M. Brewer and G. Weber, The reversible dissociation of yeast enolase, Proc. Natl. Acad. Sci. USA 59 (1968), 216-223.
2. J.M. Brewer T. Fairwell, J. Travis and R.E. Lovins, An investigation of the subunit structure of yeast enolase, Biochemistry 9 (1970), 1011-1016.
3. L.D. Faller and A.M. Johnson, Direct measurement of proton release by yeast enolase upon binding magnesium ions, FEBS Lett. 44 (1974), 298-301.
4. J.M. Brewer, Yeast enolase: mechanism of activation by metal ions, CRC Crit. Rev. Biochem. 11 (1981), 209-254.
5. C.C. Chin, J. M. Brewer and F. Wold, The amino acid sequence of yeast enolase, J. Biol. Chem. 256 (1981), 1377-1384.
6. 2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-Å resolution, Biochemistry 33 (1994) 9333-9342.
7. F. Wold, Enolase, in: The Enzymes, P.D. Boyer, ed., 3rd edn, Vol. 5, Academic Press, New York, 1971, pp. 499-538.
8. D.P. Hanlon and E.W. Westhead, Kinetic studies on the activation of yeast enolase by divalent cations, Biochemistry 8 (1969), 4255-4260.
9. L.D. Faller, B.M. Baroudy, A.M. Johnson and R.X. Ewall, Magnesium ion requirements for yeast enolase activity, Biochemistry 16 (1977), 3864-3869.
10. 6 topology, J. Biol. Chem. 264 (1989), 3685-3693.
11. B. Stec and L. Lebioda, Refined structure of yeast apo-enolase at 2.25 Å resolution, J. Mol. Biol. 211 (1990), 235-248.
12. 8 barrels: implications for the evolution of metabolic pathways, J. Mol. Biol. 303 (2000), 627-640.
13. B.E. Bowler, A. Dong and W.S. Caughey, Characterization of the guanidine-HCl denaturation state of iso-1-cytochrome c by infrared spectroscopy, Biochemistry 33 (1974), 2402-2408.
14. A. Dong, S.J. Prestrelski and J.F. Carpenter, Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation, J. Pharm. Sci. 84 (1995), 415-424.
15. A. Dong, T.W. Randolph and J.E Carpenter, Entrapping intermediates of thermal aggregation in alpha-helical proteins with low concentration of guanidine hydrochloride, J. Biol. Chem. 275 (2000), 27 689-27 693.
16. W. Shliebs, N. Thanki, R. Jaenicke and R. Wierenga, A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability, Biochemistry 36 (1997), 9655-9662.
17. M. Alvarez, J.P. Zeelen, V. Mainfroid, F. Rentier-Delrue, J.A. Martial, L. Wyns, R.K. Wierenga and D. Maes, Triosephosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus, J. Biol. Chem. 273 (1998), 2199-2206.
18. B. Gopal, S.S. Ray, R.S. Gokhale, H. Balaram, M.R.N. Murthy and P. Balaram, Cavity-creating mutation at the dimer interface of Plasmodium falciparum triosephosphate isomerase: Restoration of stability by disulfide cross-linking of subunits, Biochemistry 38 (1999), 478-486.
19. A.W.M. Rietveld and S.T. Ferreira, Kinetics and energetics of subunit dissociation/unfolding of TIM: the importance of oligomerization for conformational persistence and chemical stability of proteins, Biochemistry 37 (1998), 933-937.
20. M.E. Chánez-Cárdenas, D.A. Fernández-Velasco, E. Vázquez-Contreras, R. Coria, G. Saab-Rincon and R. Pérez-Montfort, Unfolding of triosephosphate isomerase from Trypanosoma brucei: identification of intermediates and insight into the denaturation pathway using tryptophan mutants, Arch. Biochem. Biophys. 399 (2002), 117-129.
21. M.J. Holland, J.P. Holland, G.P. Thill and K.A. Jackson, The primary structures of two yeast enolase genes. Homology between the 5′ noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes, J. Biol. Chem. 256 (1981), 1285-1395.
22. Y. Nozaki, The preparation of guanidine hydrochloride, Methods Enzymol. XXVI (1972), Part C, pp. 43-50.
23. A. Dong and W.S. Canghey, Infrared methods for study of hemoglobin reactions and structures, Methods Enzymol. 232 (1994), 139-175.
24. A. Dong, P. Huang and W.S. Caughey, Protein secondary structures in water from second-derivative amide I infrared spectra, Biochemistry 29 (1990), 3303-3308.
25. A. Dong, B. Caughey, W.S. Caughey, K.S. Bhat and J.E. Coe, Secondary structure of the pentraxin female protein in water determined by infrared spectroscopy: effects of calcium and phosphorylcholine, Biochemistry 31 (1992), 9364-9370.
26. B.S. Kendrick, A. Dong, S.D. Allison, M.C. Manning and J.E Carpenter, Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states, J. Pharm. Sci. 85 (1996), 155-158.
27. S.J. Prestrelski, N. Tedeschi, T. Arakawa and J.F. Carpenter, Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers, Biophys. J. 65 (1993), 661-671.
28. S.J. Prestrelski, T. Arakawa and J.F. Carpenter, Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II. Structural studies using infrared spectroscopy, Arch. Biochem. Biophys. 303 (1993), 465-473.
29. S. Krimm and J. Bandekar, Vibrational spectroscopy and conformation of peptides, polypeptides and proteins, Adv. Protein. Chem. 38 (1986), 181-364.
30. H. Susi and D.M. Byler, Resolution-enhanced Fourier transform infrared spectroscopy of enzymes, Methods Enzymol. 130 (1986), 290-311.
31. B.R. Singh, Basic aspects of the technique and applications of infrared spectroscopy of peptides and proteins, in: Infrared Analysis of Peptides and Proteins, Principles and Applications, B.R. Singh, ed., ACS Symposium Series 750 (2000), pp. 2-37.
32. Y.N. Chirgadze, O.V. Fedorov and N.P. Trushina, Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water, Biopolymers 14 (1975), 679-694.
33. S.J. Prestrelski, D.M. Byler and M.N. Liebman, Comparison of various molecular forms of bovine trypsin: correlation of infrared spectra with X-ray crystal structures, Biochemistry 30 (1991), 133-143.
34. C.L. Wilder, A.D. Friederich, R.O. Potts, G.O. Daumy and M. L. Francoeur, Secondary structural analysis of two recombinant murine proteins, interleukins 1α and 1β: is infrared spectroscopy sufficient to assign structure?, Biochemistry 31 (1992), 27-31.
35. P.S. Kim and R.L. Baldwin, Intermediates in the folding reactions of small proteins, Annu. Rev. Biochem. 59 (1990), 631-660.
36. K.A. Dill and D. Shortle, Denatured states of proteins, Annu. Rev. Biochem. 60 (1991), 795-825.
37. D. Shortle, The denatured state (the other half of the folding equation) and its role in protein stability, FASEB J. 10 (1996), 27-34.
38. J.W. Kelly, Alternative conformations of amyloidogenic proteins govern their behavior, Curr. Opin. Struct. Biol. 6 (1996), 11-17.
39. C.M. Dobson, Protein misfolding, evolution and disease, Trends Biochem. Sci. 24 (1999), 329-332.
40. J.D. Sipe, Amyloidosis, Ann. Rev. Biochem. 61 (1992), 947-975.
41. R.W. Carrell and B. Gooptu, Conformational changes and disease - serpins, prions and Alzheimer's, Curr. Opin. Struct. Biol. 8 (1998), 799-809.
42. E.H. Koo, P.T. Lansbury Jr. and J.W. Kelly, Amyloid diseases: abnormal protein aggregation in neurodegeneration, Proc. Natl. Acad. Sci. USA 96 (1999), 9989-9990.
43. 8 proteins using hydrogen-bonding pattern, J. Mol. Biol. 244 (1994), 168-182.
44. A.E. Todd, C.A. Orengo and J.M. Thornton, Evolution of function in protein superfamilies, from a structural perspective, J. Mol. Biol. 307 (2001), 1113-1143.
45. J. Sun and N.S. Sampson, Understanding protein lids: kinetic analysis of active hinge mutants in triosephosphate isomerase, Biochemistry 38 (1999), 11 474-11 481.
46. H. Susi and D.M. Byler, Fourier transform infrared study of proteins with parallel β-chains, Arch. Biochem. Biophys. 258 (1987), 465-469.
47. S. Krimm and A.M. Dwivedi, Infrared spectrum of the purple membrane: clue to a proton conduction mechanism?, Science 216 (1982), 407-408.
48. M. Duñach, E. Padros, A. Muga and L.R. Arrondo, Biochemistry 28 (1989), 8940-8945.
49. 10- and α-helices and β-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy, Biochemistry 30 (1991), 6541-6548.
50. 10-helical-octapeptides, Biopolymers 25 (1986), 79-89.
51. A. Dong, B.S. Kendrick, L. Kreilgård, J. Matsuura, M.C. Manning and J.F. Carpenter, Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution, Arch. Biochem. Biophys. 347 (1997), 213-220.
52. A. Dong, J.D. Meyer, J.L. Brown, M.C. Manning and J.F. Carpenter, Comparative Fourier transform infrared and circular dichroism spectroscopic analysis of α 1-proteinase inhibitor and ovalbumin in aqueous solution, Arch. Biochem. Biophys. 383 (2000), 148-155.
53. V. Mainfroid, P. Terpstra, M. Beauregard, J.-M. Frère, S.C. Mande, W.G.J. Hol, J.A. Martial and K. Goraj, Three hTIM mutants that provide new insights on why TIM is a dimer, J. Mol. Biol. 257 (1996), 441-456.
54. C.G. Benítez-Cardoza, A. Rojo-Domínguez andA. Hernández-Arana, Temperature-induced denaturation and renaturation of triosephosphate isomerase from Saccharomyces cerevisiae: Evidence of dimerization coupled to refolding of the thermally unfolded protein, Biochemistry 40 (2001), 9049-9058.
55. R.S. Gokhale, S.S. Ray, H. Balaram and P. Balaram, Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant, Biochemistry 38 (1999), 423-431.
56. D.O. Alonso and K.A. Dill, Solvent denaturation and stabilization of globular proteins, Biochemistry 30 (1991), 5974-5985.
57. L. Lebioda and B. Stec, Crystal structure of holoenolase refined at 1.9 Å resolution: trigonal-bipyramidal geometry of the cation binding site, J. Am. Chem. Soc. 111 (1989), 8511-8513.