Temperature control for kinetic refolding of heat-denatured ovalbumin

Protein Science

Volumn 6, Issue 7, 1997, Pages 1491-1502

  Tani, Fumito ^a   Shirai, Nobuaki ^a   Onishi, Toru ^a,c   Venelle, Franck ^a   Yasumoto, Kyoden ^a   Doi, Etsushiro ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b KINKI UNIVERSITY   (Japan)

^c KANEKA CORPORATION   (Japan)

Author keywords

Alternative cooling process; Heat denaturation; Kinetic barrier; Kinetically trapped intermediate; Non native disulfide pairing; Ovalbumin; Temperature control

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; DISULFIDE; OVALBUMIN; SERINE PROTEINASE INHIBITOR; TRYPSIN;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; TEMPERATURE DEPENDENCE; THERMAL EXPOSURE;

EID: 0030743517     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060713     Document Type: Article

References (60)

1. Ackers GK. 1967. A new calibration procedure for gel filtration columns. J Biol Chem 242:3237-3238.
2. Baldwin RL. 1995. The nature of protein folding pathways: The classical versus the new view. J Biomol NMR 5:103-109.
3. Barrick D, Baldwin RL. 1993. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci 2:869-876.
4. Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG. 1995. Funnels, pathways and the energy landscape of protein folding: A synthesis. Proteins Struct Funct Genet 27:167-195.
5. Bycroft M, Matouschek A, Kellis JT Jr, Serrano L, Fersht AR. 1990. Detection and characterization of a folding intermediate in barnase by NMR. Nature 346:488-490.
6. Corbett RJT, Roche RS. 1984. Use of high-speed size-exclusion chromatography for the study of protein folding and stability. Biochemistry 23:1888-1894.
7. Creighton TE. 1986. Disulfide bonds as probes of protein folding pathways. Methods Enzymol 131:83-106.
8. Creighton TE. 1988. Toward a better understanding of protein folding pathways. Proc Natl Acad Sci USA 85:5082-5086.
9. Creighton TE. 1994. The energetic ups and downs of protein folding. Nature Struct Biol 1:135-138.
10. Dill KA. 1985. Theory for the folding and stability of globular proteins. Biochemistry 24:1501-1509.
11. Dill KA, Bromberg S, Yue K, Fiebig KM, Yee DP, Thomas PD, Chan HS. 1995. Principles of protein folding - A perspective from simple exact models. Protein Sci 4:561-602.
12. Dobson CM, Evans PA, Radford SE. 1994. Understanding how proteins fold: The lysozyme story so far. Trends Biochem Sci 19:31-37.
13. Dolgikh DA, Gilmanshin RI, Brazhnikov EV, Bychkova VE, Semisotonov GV, Venyaminov SYu, Ptitsyn OB. 1981. α-Lactalbumin: Compact state with fluctuating tertiary structure? FEBS Lett 136:311-315.
14. Elöve GA, Bhuyan AK, Roder H. 1994. Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands. Biochemistry 33:6925-6935.
15. Fersht AR. 1995. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92:10869-10873.
16. Gettins PGW, Patston PA, Olson ST. 1996. Serpins: Structure, function and biology. Austin, Texas: R.G. Landes Company.
17. Gutin AM, Abkevich VI, Shakhnovich EI. 1995. Is burst hydrophobic collapse necessary for protein folding? Biochemistry 34:3066-3076.
18. Honeycutt JD, Thirumalai D. 1990. Metastability of the folded states of globular proteins. Proc Natl Acad Sci USA 87:3526-3529.
19. Hua QX, Gozani SN, Chance RE, Hoffman JA, Frank BH, Weiss MA. 1995. Structure of a protein in a kinetic trap. Nature Struct Biol 2:129-138.
20. 1-antitrypsin for structure and function of serpins. Biochemistry 25:8951-8966.
21. Hughson FM, Wright PE, Baldwin RL. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548.
22. Ikeguchi M, Kuwajima K, Mitani M, Sugai S. 1986. Evidence for identity between equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reaction of α-lactalbumin and lysozyme. Biochemistry 25:6965-6972.
23. Imahori K. 1960. Rotatory behavior of protein denaturation. Biochim Biophys Acta 37:336-341.
24. Itzhaki LS, Evans PA, Dobson CM, Radford SE. 1994. Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes. Biochemistry 33:5212-5220.
25. Jennings PA, Wright PE. 1993. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262:892-896.
26. Kataoka M, Goto Y. 1996. X-ray solution scattering studies of protein folding. Folding & Design 1:107-114.
27. Khorasanizadeh S, Peters ID, Butt TR, Roder H. 1993. Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry 32:7054-7063.
28. Kim PS, Baldwin RL. 1982. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Annu Rev Biochem 57:459-489.
29. Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59:631-660.
30. Klausner RD, Kempf C, Weinstein JN, Blumenthal R, Renswoude JV. 1983. The folding of ovalbumin. Biochem J 212:801-810.
31. Konishi Y, Ooi T, Scheraga HA. 1982. Regeneration of RNase A from the reduced protein: Models of regeneration pathways. Proc Natl Acad Sci USA 79:5734-5738.
32. Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Ciystallogr 24:946-950.
33. Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins Struct Funct Genet 6:87-103.
34. Kuwajima K, Yamaya H, Miwa S, Sugai S, Nagamura T. 1987. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett 221:115-118.
35. Labhardt AM. 1982. Secondary structure in ribonuclease. I. Equilibrium folding transition seen by amide circular dichroism. J Mol Biol 157:331-355.
36. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
37. Matouschek A, Serrano L, Fersht AR. 1992a. The folding of an enzyme: IV. Structure of an intermediate in the refolding of barnase analyzed by a protein engineering procedure. J Mol Biol 224:819-836.
38. 2H exchange nuclear magnetic resonance studies on the folding pathway of barnase: Complementarity to and agreement with protein engineering studies. J Mol Biol 224:837-845.
39. Matthews CR. 1993. Pathways of protein folding. Annu Rev Biochem 62:653-683.
40. Merritt EA, Murphy EP. 1994. Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr D 50:869-873.
41. Miller JA, Narhi LO, Hua QX, Rosenfeld R, Arakawa T, Rohde M, Prestrelski S, Lauren S, Stoney KS, Tsai L, Weiss MA. 1993. Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: A bifurcating protein-folding pathway. Biochemistry 52:5203-5213.
42. Ohgushi M, Wada A. 1983. "Molten-globule state": A compact form of globular proteins with mobile side chains. FEBS Lett 164:21-24.
43. Ottesen M, Wallevik K. 1968. Use of the pH-stat for measuring the denaturation of ovalbumin in acid solutions. Biochim Biophys Acta 160:262-264.
44. Ptitsyn OB. 1987. Protein folding: Hypotheses and experiments. J Protein Chem 6:273-293.
45. Ptitsyn OB. 1992. The molten globule state. In: Creighton TE, ed. Protein folding. New York: W.H. Freeman and Company. pp 243-300.
46. Radford SE, Dobson CM. 1995. Insights into protein folding using physical techniques: Studies of lysozyme and a-lactalbumin. Phil Trans R Soc Lond B 348:17-25.
47. Radford SE, Dobson CM, Evans PA. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358:302-307.
48. Roder H. Elöve GA, Englander SW. 1988. Structural characterization of folding intermediate in cytochrome c by H-exchange labeling and proton NMR. Nature 335:700-704.
49. Simpson RB, Kauzman W. 1953. The kinetics of protein denaturation. I. The behavior of the optical rotation of ovalbumin in urea solutions. J Am Chem Soc 75:5139-5152.
50. Sörensen SPL, Höyrup M. 1915. Studies on proteins. I. On the preparation of egg-albumin solutions of well-defined composition, and on the analytical methods used. Compt Rend Trav Lab Carlsberg 12:12-67.
51. Sosnick TR, Mayne L, Hiller R, Englander SW. 1994. The barriers in protein folding. Nature Struct Biol 1:149-156.
52. Stein PE, Leslie AG, Finch JT, Carrell RW. 1991. Crystal structure of uncleaved ovalbumin at 1.95 Å resolution. J Mol Biol 221:941-959.
53. Takahashi N, Hirose M. 1992. Reversible denaturation of disulfide-reduced ovalbumin and its reoxidation generating the native cystine cross-link. J Biol Chem 267:11565-11572.
54. Tatsumi E, Takahashi N, Hirose M. 1994. Denatured state of ovalbumin in high concentrations of urea as evaluated by disulfide rearrangement analysis. J Biol Chem 269:28062-28067.
55. Udgaonkar JB, Baldwin RL. 1990. Early folding intermediate of ribonuclease A. Proc Natl Acad Sci USA 87:8197-8201.
56. Weissman JS, Kim PS. 1991. Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253:1386-1393.
57. Weissman JS, Kim PS. 1992. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci USA 89:9900-9904.
58. Wetlaufer DB. 1973. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc Natl Acad Sci USA 70:697-701.
59. Wolynes PG, Onuchic JN, Thirumalai D. 1995. Navigating the folding routes. Science 267:1619-1620.
60. Wu LC, Peng ZY, Kim PS. 1995. Bipartite structure of the α-lactalbumin molten globule. Nature Struct Biol 2:281-286.