Acceleration of the folding of hen lysozyme by trifluoroethanol

Journal of Molecular Biology

Volumn 265, Issue 2, 1997, Pages 112-117

  Lu, Hui ^a   Buck, Matthias ^a   Radford, Sheena E ^a   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Hydrogen bonding; Hydrophobic interaction; Kinetic traps; Partially folded states; Rate enhancement

Indexed keywords

GUANIDINE; LYSOZYME; TRIFLUOROETHANOL;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE; HEN; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 0031575421     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0715     Document Type: Article

References (40)

1. Aune K. C., Tanford C. Thermodynamics of the denaturation of lysozyme by Guanidine Hydrochloride. II. Dependence on denaturant concentration at 25° Biochemistry. 8:1969;4586-4590.
2. Buck M., Radford S. E., Dobson C. M. A partially folded state of HEWL in TFE: structural characterisation and implications for protein folding. Biochemistry. 32:1993;669-678.
3. Buck M., Schwalbe H., Dobson C. M. Characterisation of conformational preferences in a partially folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol. Biochemistry. 34:1995;13219-13232.
4. 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol. J. Mol. Biol. 257:1996;669-683.
5. Cammers-Goodwin A., Allen T. J., Oslick S. L., McClure K. F., Lee J. H., Kemp D. S. Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J. Am. Chem. Soc. 118:1996;3082-3090.
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. 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.
8. Dyson H. J., Merutka G., Waltho J. P., Lerner R. A., Wright P. E. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226:1992;795-817.
9. Ittah V., Haas E. Non-local interactions stabilise long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor. Biochemistry. 34:1995;4493-4506.
10. Itzhaki L. S., Evans P. A. Solvent isotope effects on the refolding kinetics of hen egg-white lysozyme. Protein Sci. 5:1996;140-146.
11. Itzhaki L. S., Evans P. A., Dobson C. M., Radford S. E. Tertiary interactions in the folding pathwayof hen lysozyme: kinetic studies using fluorescent probes. Biochemistry. 33:1994;5212-5220.
12. Itzhaki L. S., Neira J. L., Ruiz-Sanz J., Prat Gay G. de, Fersht A. R. Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2. J. Mol. Biol. 254:1995;289-304.
13. Jackson S. E., Fersht A. R. Folding of chymotrypsin inhibitor 2.A1. Evidence for a two-state transition. Biochemistry. 30:1991;10428-10435.
14. Kiefhaber T. Kinetic traps in lysozyme folding. Proc. Natl Acad. Sci. USA. 92:1995;9029-9033.
15. Kim P. S., Baldwin R. L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:1990;631-660.
16. Kragelund B. B., Robinson C. V., Knudsen J., Dobson C. M., Poulsen F. M. Folding of a 4-helix bundle: studies of acyl-coenzyme-A binding-protein. Biochemistry. 34:1995;7217-7224.
17. Lehrman S. R., Tuls J. L., Lund M. Peptide α-helicity in aqueous trifluoroethanol: correlations with predicted α-helicity and the secondary structure of the corresponding regions of bovine growth hormone. Biochemistry. 29:1990;5590-5596.
18. Matouschek A., Kellis J. T., Serrano L., Bycroft M., Fersht A. R. Transient folding intermediates characterized by protein engineering. Nature. 346:1990;440-445.
19. Matthews C. R. Pathways of protein folding. Annu. Rev. Biochem. 62:1993;653-683.
20. Miranker A. D., Dobson C. M. Collapse and cooperativity in protein folding. Curr. Opin. Struct. Biol. 6:1996;31-42.
21. Nelson J. W., Kallenbach N. R. Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol solutions. Proteins: Struct. Funct. Genet. 1:1986;211-217.
22. Peng Z. Y., Kim P. S. A protein dissection study of a molten globule. Biochemistry. 33:1994;2136-2141.
23. Pfeil W., Privalov P. L. Thermodynamic investigation of lysozyme. Biophys. Chem. 4:1976;41-50.
24. Plaxco K. W., Dobson C. M. Time resolved biophysical methods in the study of protein folding. Curr. Opin. Struct. Biol. 6:1996;630-636.
25. Prat Gay G. de, 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. 92:1995;3683-3686.
26. Radford S. E., Dobson C. M. Insights into protein folding using physical techniques: studies of lysozyme and α-lactalbumin. Phil. Trans. Roy. Soc. Ser. B. 348:1995;17-25.
27. Radford S. C., Dobson C. M., Evans P. A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
28. Rothwarf D. M., Scheraga H. A. The role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry. In the press:1996.
29. Sali A., Shakhnovich E., Karplus M. How does a protein fold? Nature. 369:1994;248-251.
30. 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.
31. Schmid F. X. Kinetics of unfolding and refolding of single-domain protein. Protein Folding. 1992;Freeman, New York.
32. Schoenbrunner N., Wey J., Engels J., Georg H., Kiefhaber T. Native-like beta structure in a trifluoroethanol induced partially folded state of the all beta-protein tendamistat. J. Mol. Biol. 260:1996;432-445.
33. 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;2473-2488.
34. Segawa S., Fukuno T., Fujiwara K., Noda Y. Local structure in unfolded lysozyme and correlation with secondary structures in the native conformation: helix-forming or -breaking propensity of peptide segments. Biopolymers. 31:1991;497-509.
35. Shin H.-C., Merutka G., Waltho J. P., Wright P. E., Dyson H. J. Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin. Biochemistry. 32:1993;6356-6364.
36. Shiraki K., Nishikawa K., Goto Y. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245:1995;180-194.
37. Thomas P. D., Dill K. A. Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation. Protein Sci. 2:1993;2050-2065.
38. Waltho J. P., Feher V. A., Merutka G., Dyson H. J., Wright P. E. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry. 32:1993;6337-6347.
39. Yang A. S., Honig B. On the pH dependence of protein stability. J. Mol. Biol. 231:1993;459-474.
40. Yang J. J., Buck M., Pitkeathly M., Kotik M., Haynie D. T., Dobson C. M., Radford S. E. Four peptides which span the entire sequence of hen lysozyme have distinct conformational properties in water and TFE: structural implications for early folding intermediates. J. Mol. Biol. 252:1995;483-491.