The Folding Mechanism of Barstar: Evidence for Multiple Pathways and Multiple Intermediates

Journal of Molecular Biology

Volumn 247, Issue 5, 1995, Pages 1013-1027

  Shastry, M C R ^a   Udgaonkar, Jayant B ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

ANS; Barstar; Folding kinetics; Molten globule; Protein folding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GUANIDINE; PROTEIN;

ARTICLE; CONTROLLED STUDY; DATA ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; REACTION ANALYSIS;

EID: 0028901085     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1994.0196     Document Type: Article

References (31)

1. Baldwin, R. L. (1993). Pulsed H/D-exchange studies of folding intermediates. Curr. Opin. Struct. Biol. 3, 84-91.
2. Brandts, J. F., Halvarson, H. R. & Brennan, M. (1975). Consideration of the possibility that the slow step in the protein denaturation reaction is due to cis-trans isomerization of proline residues. Biochemistry, 14, 4953-4963.
3. de Prat Gay G. & Fersht, A. R. (1994). Generation of family of protein fragments for structure folding studies. 1. Folding complimentation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue. Biochemistry, 33, 7957-7963.
4. Dolgikh, D. A., Abaturov, L. K., Bolotina, I. A., Brazhnikov, E. V, Bushev, V. N., Bychkova, V. E., Gilmanshin, R. I., Lebedev, Y. O., Semisotnov, G. V., Yiktopulo, E. I. & Ptitsyn, O. B. (1985). Compact state of a protein molecule with pronounced small scale mobility: bovine a-lactalbumin. Eur. J. Biophys. 13, 109-121
5. Evans, P. A. & Radford, S. E. (1994). Probing the structure of folding intermediates. Curr. Opin. Struct. Biol. 4, 100-106.
6. Garel, J. R. & Baldwin, R. L. (1973). Both the fast- and slow-refolding reactions of ribonuclease A yield native enzyme. Proc. Nat. Acad. Sci., U.S.A. 70, 3347-3350.
7. Guillet, V., Lapthorn, A., Hartley R. W. & Mauguen, Y (1993). Recognition between a bacterial ribonuclease barnase, and its natural inhibitor, barstar. Structure, 1, 165-176.
8. Hammes, G. G. (1982). Enzyme Catalysis and Regulation, Academic Press, New York.
9. Hartley R. W. (1988). Barnase and barstar. Expression of its cloned inhibitor prevents expression of a cloned ribonuclease. J. Mol. Biol. 202, 913-915.
10. Khurana, R. & Udgaonkar, J. B. (1994). Equilibrium unfolding studies of barstar: evidence for an alternative conformation which resembles a molten globule. Biochemistry, 33, 106-115.
11. Kiefhaber, T., Kohler, H. A. & Schmid, F. X. (1992). Kinetic coupling between protein folding and prolyl polymerization. I. Theoretical models. J. Mol. Biol. 224, 217-229.
12. Kim, P S. & Baldwin, R. L. (1990). Intermediates in the folding reaction of small proteins. Annu. Rev. Biochem. 59, 631-660.
13. Kuwajima, K., Hiraoka, Y, Ikeguchi, M. & Sugai, S. (1985). Comparison of the transient folding intermediates in lysozyme and a -lactalbumin. Biochemistry, 24, 874-881.
14. Kuwajima, K., Yamaya, H., Miwas, S., Sugai, S. & Nagamura, T. (1987). Rapid formation of secondary structure frame work in protein folding studied by stopped-flow circular dichroism. FEBS Letters, 221, 115-118.
15. 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Biochemistry, 33, 8866-8877.
16. Matouschek, A., Kellis, J. T., Serrano, L., Bycroft, M. & Fersht, A. R. (1990). Transient folding intermediates characterized by protein engineering. Nature (London), 346, 440-445.
17. Matthews, C. R. (1993). Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683.
18. Mullins, L., Pace, C. N. & Raushel, F. (1993). Folding intermediates by hydrogen-deuterium amide exchange two-dimensional NMR spectroscopy. Biochemistry 32, 6152-6156.
19. Ptitsyn, O. B. (1994). Kinetic and equilibrium intermediates in protein folding. Protein Eng. 7, 593-596.
20. Roder, H., Elove, G. A. & Englander, S. W. (1988). Structural characterization of the folding intermediate in cytochrome C by H-exchange labelling and proton NMR. Nature (London), 335, 700-704.
21. Schmid, F. X. (1983). Mechanism of folding of ribonuclease A. Slow folding is a sequential reaction via structural intermediates. Biochemistry, 22, 4690-4696.
22. Schmid, F. X. (1986). Fast-folding and slow-folding forms of unfolded proteins. Methods Enzymol. 131, 70-82.
23. Schreiber, G. & Fersht, A. R. (1993). The refolding of cis and trans-peptidyl prolyl isomers of barstar. Biochemistry, 32, 11195-11203.
24. Semisotnov, G. V., Radionova, N. A., Kutyshenko, V. P., Ebert, B., Blanck, J. & Ptitsyn, O. B. (1987). Sequential mechanism of refolding of carbonic anhydrase B. FEBS Letters, 224, 9-13.
25. Shastry M. C. R., Agashe, V. R. & Udgaonkar, J. B. (1994). Quantitative analysis of the kinetics of renaturation and denaturation of barstar in the folding transition zone. Protein Sci. 3, 1409-1417.
26. Stryer L. (1965). The interaction of naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13, 482-495.
27. Swaminathan, R., Periasamy N., Udgaonkar, J. B. & Krishnamoorthy G. (1994). Molten globule-like conformation of barstar: a study by fluorescence dynamics. J. Phys. Chem. 98, 9270-9278.
28. Tanford, C. (1970). Proteindenaturation. PartC.Theoretical models for the mechanism of denaturation. Advan. Protein Chem. 21, 1-95.
29. Udgaonkar, J. B. & Baldwin, R. L. (1988). NMR evidence for an early intermediate in the folding pathway of ribonuclease A. Nature (London), 335, 694-699.
30. Udgaonkar, J. B. & Baldwin, R. L. (1990). Early folding intermediate of ribonuclease A. Proc. Nat. Acad. Sci., U.S.A. 87, 8197-8201.
31. Szabo, Z. G. (1969). Kinetic characterization of complex reaction systems. In Comprehensive Chemical Kinetics (Bamford, C. H. & Tipper, C. F. H., eds), Vol. 2, pp. 1-80, Elsevier, New York.