Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process

Journal of Molecular Biology

Volumn 267, Issue 5, 1997, Pages 1068-1074

  Matagne, André ^a   Radford, Sheena E ^a   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Folding intermediates; Hen egg white lysozyme; Multiple pathways; Protein folding; Stopped flow fluorescence

Indexed keywords

ENZYME INHIBITOR; LYSOZYME;

ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN TRANSPORT;

EID: 0031576990     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0963     Document Type: Article

References (38)

1. Alexander P., Orban J., Bryan P. Kinetic analysis of folding and unfolding of the 56 amino acid IGG-binding domain of streptococcal protein G. Biochemistry. 31:1992;7243-7248.
2. Baldwin R. L. The nature of protein folding pathways: the classical view versus the new view. J. Biomol. NMR. 5:1995;103-109.
3. Baldwin R. L. On-pathway versus off-pathway folding intermediates. Folding and Design. 1:1996;R1-R8.
4. Branden C., Tooze J. Introduction to Protein Structure. 1991;Garland Publishing, Inc. New York and London.
5. Briggs M. S., Roder H. Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc. Natl Acad. Sci. USA. 89:1992;2017-2021.
6. Chaffotte A. F., Guillou Y., Goldberg M. E. Kinetic resolution of peptide bond and side chain far UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry. 31:1992;9694-9702.
7. Chan H. S., Dill K. A. Transition states and folding dynamics of proteins and heteropolymers. J. Chem. Phys. 100:1994;9238-9257.
8. Creighton T. E. Protein folding. Biochem. J. 270:1990;1-16.
9. Creighton T. E. Proteins, Structures and Molecular Properties. 1993;W.H. Freeman and Co. New York.
10. Dobson C. M. Characterization of protein folding intermediates. Curr. Opin. Struct. Biol. 1:1991;22-27.
11. Dobson C. M., Evans P. A., Radford S. E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19:1994;31-37.
12. Fersht A. R. Protein folding and stability: the pathway of folding of barnase. FEBS Letters. 325:1993;5-16.
13. Fersht A. R. Characterizing transition-states in protein-folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5:1995;79-84.
14. Goux W. J., Hooker T. M., Jr. The chiroptical properties of proteins. II. Near-Ultraviolet circular dichroism of lysozyme. Biopolymers. 19:1980;2191-2208.
15. Hooke S. D., Eyles S. J., Miranker A., Radford S. E., Robinson C. V., Dobson C. M. The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme. Biochemistry. 33:1994;5867-5876.
16. Huang G. S., Oas T. G. Submillisecond folding of monomeric λ repressor. Proc. Natl. Acad. Sci. USA. 92:1995;6878-6882.
17. Itzhaki L. S., Evans P. A., Dobson C. M., Radford S. E. Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry. 33:1994;5212-5220.
18. Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two state transition. Biochemistry. 30:1991;10428-10435.
19. Karplus M., Sali A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5:1995;58-73.
20. Kato S., Okamura M., Shimamoto N., Utiyama H. Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme. Biochemistry. 20:1981;1080-1085.
21. Kato S., Shimamoto N., Utiyama H. Identification and characterization of the direct folding process of hen egg white lysozyme. Biochemistry. 21:1982;38-43.
22. Khorasanizadeh S., Peters I. D., Roder H. Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry. 32:1993;7054-7063.
23. Kiefhaber T. Kinetic traps in lysozyme folding. Proc. Natl Acad. Sci. USA. 92:1995;9029-9033.
24. Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
25. Kragelund B. B., Robinson C. V., Knudsen J., Dobson C. M., Poulsen F. M. Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. Biochemistry. 34:1995;7217-7224.
26. Matthews C. R. Pathways of protein folding. Annu. Rev. Biochem. 62:1993;653-683.
27. Miranker A., Dobson C. R. Collapse and cooperativity in protein folding. Curr. Opin. Struct. Biol. 6:1996;31-42.
28. Miranker A., Radford S. E., Karplus M., Dobson C. M. Demonstration by NMR of folding domains in lysozyme. Nature. 349:1991;633-636.
29. Miranker A., Robinson C. V., Radford S. E., Aplin R. T., Dobson C. M. Detection of transient protein folding populations by mass spectrometry. Science. 262:1993;896-900.
30. Radford S. E., Dobson C. M., Evans P. A. The folding pathway of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
31. Rothwarf D. M., Scheraga H. A. Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry. 35:1996;13797-13807.
32. Sali A., Shakhnovich E., Karplus M. How does a protein fold? Nature. 369:1994;248-251.
33. Schindler T., Herrler M., Marahiel M. A., Schmid F. X. Extremely rapid protein folding in the absence of intermediates. Nature Struct. Biol. 2:1995;663-673.
34. Segawa S., Sugihara M. Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state. Biopolymers. 23:1984;2437-2488.
35. Sosnick T. R., Mayne L., Hiller R., Englander S. W. The barriers in protein folding. Nature Stuct. Biol. 1:1994;149-156.
36. Stuart D. I., Acharya K. R., Walker N. P. C., Smith S. G., Lewis M., Philips D. C. α-lactalbumin possesses a novel calcium binding loop. Nature. 324:1986;84-87.
37. Van Landshoot A., Lootiens F. G., Clegg R. M., Sharon N., De Bruyne C. K. Binding of 4-methylumbelliferyl N -acetyl-chitooligosaccharides to wheat-germ agglutinin. A reinvestigation of equilibrium studies. Eur. J. Biochem. 79:1977;275-283.
38. Viguera A. R., Martinez J. C., Filimonov V. V., Mateo P. L., Serano L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry. 33:1994;2142-2150.