A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale

Biophysical Journal

Volumn 74, Issue 5, 1998, Pages 2714-2721

  Shastry, M C Ramachandra ^a   Luck, Stanley D ^a,c   Roder, Heinrich ^a,b  

^a FOX CHASE CANCER CENTER   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c DUPONT COMPANY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; ANALYTIC METHOD; APPARATUS; ARTICLE; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; FLUORESCENCE; MONITORING; PROTEIN FOLDING;

MUS; PHASEOLUS (ANGIOSPERM);

EID: 0031969090     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77977-9     Document Type: Article

References (40)

1. Berger, R. L., B. Balko, W. Borcherdt, and W. Friauf. 1968b. High speed optical stopped-flow apparatus. Rev. Sci. Instrum. 39:486-493.
2. Berger, R. L., B. Balko, and H. F. Chapman. 1968a. High resolution mixer for the study of the kinetics of rapid reactions in solution. Rev. Sci. Instrum. 39:493-498.
3. Brems, D. N., and E. Stellwagen. 1983. Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c. J. Biol. Chem. 258:3655-3660.
4. Brissette, P., D. P. Ballou, and V. Massey. 1989. Determination of the dead time of a stopped-flow fluorometer. Anal. Biochem. 181:234-238.
5. Chan, C-K., Y. Hu, S. Takahashi, D. L. Rousseau, W. A. Eaton, and J. Hofrichter. 1997. Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc. Natl. Acad. Sci. USA. 94:1779-1784.
6. Chance, B. 1940. The accelerated-flow method for rapid reactions. I. Anal. J. Franklin Inst. 229:455-613.
7. Colón, W., G. A. Elöve, L. P. Wakem, F. Sherman, and H. Roder. 1996. Side chain packing of the N-and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry. 35:5538-5549.
8. Elöve, G. A., A. K. Bhuyan, and H. Roder. 1994. Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry. 33:6925-6935.
9. Elöve, G. A., A. F. Chaffotte, H. Roder, and M. E. Goldberg. 1992. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry. 31:6876-6883.
10. Fersht, A. 1985. Enzyme Structure and Mechanism. W. H. Freeman and Company, New York.
11. Gibson, Q. H., and E. Antonini. 1966. kinetics of heme-protein intractions. In Hemes and Hemeproteins. Academic Press, New York. 67-78.
12. Gibson, Q. H., and L. Milnes. 1964. Biochem. J. 91:161.
13. Hartridge, H., and F. J. W. Roughton. 1923. Method of measuring the velocity of very rapid chemical reactions. Proc. R. Soc. Lond. A Math. Phys. Sci. 104:376-394.
14. Jones, C. M., E. R. Henry, Y. Hu, C.-K. Chan, S. D. Luck, A. Bhuyan, H. Roder, J. Hofrichter, and W. A. Eaton. 1993. Fast events in protein folding initiated by nanosecond laser photolysis. Proc. Natl. Acad. Sci. USA. 90:11860-11864.
15. Khorasanizadeh, S., I. D. Peters, and H. Roder. 1996. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3:193-205.
16. Kim, P. S., and R. L. Baldwin. 1990. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631-660.
17. Kletenik, Y. B. 1963. A mixer for investigating the kinetics of rapid reactions in solutions by the flow method. J. Phys. Chem. USSR. 37:638-640.
18. 2+ binding on the folding kinetics of α-lactalbumin. J. Mol. Biol. 206:547-561.
19. Kuwajima, K., H. Yamaya, S. Miwa, S. Sugai, and T. Nagamura. 1987. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Lett. 221:115-118.
20. Matthews, C. R. 1993. Pathways of protein folding. Annu. Rev. Biochem. 62:653-683.
21. Miranker, A. D., and C. M. Dobson. 1996. Collapse and cooperativity in protein folding. Curr. Opin. Struct. Biol. 6:31-42.
22. Moskowitz, G. W., and R. L. Bowman. 1966. A multicapillary mixer of solutions. Science. 153:428-429.
23. Paeng, K., I. Paeng, and J. Kincaid. 1994. Time-resolved resonance Raman spectroscopy using a fast mixing device. Anal. Sci. 10:157-159.
24. Park, S.-H., K. T. O'Neil, and H. Roder. 1997. An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core. Biochemistry. 36:14277-14283.
25. Parker, M. J., J. Spencer, and A. R. Clarke. 1995. An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253:771-786.
26. Paul, C., K. Kirschner, and G. Haenisch. 1980. Calibration of stopped-flow spectrophotometers using a two-step disulfide exchange reaction. Anal. Biochem. 101:442-448.
27. Peterman, B. F. 1979. Measurement of the dead time of a fluorescence stopped-flow instrument. Anal. Biochem. 93:442-444.
28. Ptitsyn, O. B. 1995. Structures of folding intermediates. Curr. Opin. Struct. Biol. 5:74-78.
29. Regenfuss, P., R. M. Clegg, M. J. Fulwyler, F. J. Barrantes, and T. M. Jovin. 1985. Mixing liquids in microseconds. Rev. Sci. Instrum. 56: 283-290.
30. Roder, H. 1989. Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol. 176:446-473.
31. Roder, H., and W. Colon. 1997. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7:15-28.
32. Roder, H., and G. A. Elöve. 1994. Early stages of protein folding. In Mechanisms of Protein Folding: Frontiers in Molecular Biology. Oxford University Press, New York. 26-55.
33. Roder, H., G. A. Elöve, and S. W. Englander. 1988. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature. 335:700-704.
34. 2. Biochemistry. 35:16852-16862.
35. Sosnick, T. R., L. Mayne, and S. W. Englander. 1996. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins. 24: 413-426.
36. Sosnick, T. R., L. Mayne, R. Hiller, and S. W. Englander. 1994. The barriers in protein folding. Nature Struct. Biol. 1:149-156.
37. Takahashi, S., Y.-c. Ching, J. Wang, and D. L. Rousseau. 1995. Microsecond generation of oxygen-bound cytochrome c oxidase by rapid solution mixing. J. Biol. Chem. 270:8405-8407.
38. Takahashi, S., S.-R. Yeh, T. K. Das, C.-K. Chan, D. S. Gottfried, and D. L. Rousseau. 1997. Folding of cytochrome c initiated by submillisecond mixing. Nature Struct. Biol. 4:44-50.
39. Tonomura, B., H. Nakatani, M. Ohnishi, J. Yamaguchi-Ito, and K. Hiromi. 1978. Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid. Anal. Biochem. 84:370-383.
40. Tsong, T. Y. 1976. Ferricytochrome c chain folding measured by the energy transfer of tryptophan 59 to the heme group. Biochemistry. 15:5467-5473.