Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering

Journal of Molecular Biology

Volumn 288, Issue 3, 1999, Pages 489-499

  Segel, Daniel J ^a   Bachmann, Annett ^b   Hofrichter, James ^c   Hodgson, Keith O ^a,d   Doniach, Sebastian ^a   Kiefhaber, Thomas ^b  

^a STANFORD UNIVERSITY   (United States)

^b UNIVERSITY OF BASEL   (Switzerland)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

^d SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

Folding intermediates; Folding kinetics; Lysozyme; Protein folding; SAXS

Indexed keywords

LYSOZYME;

ARTICLE; CONTROLLED STUDY; HYDROPHOBICITY; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; RADIATION SCATTERING; SYNCHROTRON;

EID: 0033532201     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2703     Document Type: Article

References (30)

1. Chaffotte A. F., Guillou Y., Goldberg M. E. Kinetic resolution of peptide bond and side-chain far-UV CD during folding of HEWL. Biochemistry. 31:1992;9694-9702.
2. Chan C.-K., Hu Y., Takahashi S., Rousseau D. L., Eaton W. A., Hofrichter J. Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc. Natl Acad. Sci. USA. 94:1997;1779-1784.
3. Chen L., Hodgson K. O., Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261:1996;658-671.
4. Chen L., Wildegger G., Kiefhaber T., Hodgson K. O., Doniach S. Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering. J. Mol. Biol. 276:1998;225-237.
5. 127)-lysozyme: a stopped-flow absorbance and fluorescence study. Biochemistry. 33:1994;11225-11236.
6. Dobson C. M. Unfolded proteins, compact states and molten globules. Curr. Opin. Struct. Biol. 2:1992;6-12.
7. Doniach S., Bascle J., Garel T., Orland H. Partially folded states of proteins: characterization by X-ray scattering. J. Mol. Biol. 254:1995;960-967.
8. Eliezer D., Chiba K., Tsuruta H., Doniach S., Hodgson K. O., Kihara H. Evidence for an associative intermediate on the myoglobin refolding pathway. Biophys. J. 65:1993;912-917.
9. Gladwin S. T., Evans P. A. Structure of very early protein folding intermediates: new insight through a variant of hydrogen exchange labeling. Fold. Design. 1:1996;407-417.
10. Glatter O., Kratky O. Small Angle X-Ray Scattering. 1982;Academic Press, New York.
11. Henry E. R., Hofrichter J. Singular value decomposition: application to analysis of experimental data. Methods Enzymol. 210:1992;129-192.
12. 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.
13. Kato S., Shimamoto N., Utijama H. Identification and characterization of the direct folding process of hen egg-white lysozyme. Biochemistry. 21:1982;38-43.
14. Kiefhaber T. Kinetic traps in lysozyme folding. Proc. Natl Acd. Sci. USA. 92:1995;9029-9033.
15. Kuwajima K., Hiraoka Y., Ikeguchui M., Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:1985;874-881.
16. Lakowicz J. R. Principles of Fluorescence Spectroscopy. 1983;Plenum Press, New York.
17. Luo Y., Kay M. S., Baldwin R. L. Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations. Nature Struct. Biol. 4:1997;925-929.
18. Morgan C. J., Miranker A., Dobson C. M. Characterization of collapsed states in the early stages of the refolding of hen lysozyme. Biochemistry. 37:1998;8473-8480.
19. Peterman B. F. Measurement of the dead-time of a fluorescence stopped-flow instrument. Anal. Biochem. 93:1979;442-444.
20. Radford S. E., Dobson C. M., Evans P. A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
21. 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.
22. Schmid F. X. Fast-folding and slow-folding forms of unfolded proteins. Meth. Enzymol. 131:1986;70-82.
23. Segel D. J., Fink A. L., Hodgson K. O., Doniach S. Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochromec. Biochemistry. 37:1998;12443-12541.
24. Semenyuk A. V., Svergun D. I. GNOM- a program for small-angle scattering data processing. J. Appl. Crystallog. 24:1991;537-540.
25. Tanford C., Aune K. C., Ikai A. Kinetics of unfolding and refolding of proteins. III. Results for lysozyme. J. Mol. Biol. 73:1973;185-197.
26. Tsuruta H., Nagamura T., Kimura K., Igarashi Y., Kajita A., Wang Z. X., Wakabayashi K., Amemiya Y., Kihara H. Stopped-flow apparatus for X-ray scattering at subzero temperature. Rev. Sci. Instruments. 60:1989;2356-2358.
27. Tsuruta H., Brennan S., Rek Z. U., Irving T. C., Tompkins W., Hodgson K. O. Wide bandpass multilayer monochromator for biological small angle scattering and fiber diffraction studies. J. Appl. Crystallog. 31:1998;672-682.
28. Wakatsuki S., Hodgson K. O., Eliezer D., Rice M., Hubbard S., Gillis N., Doniach S. Small-angle x-ray-scattering diffraction system for studies of biological and other materials at the Stanford-Synchrotron-Radiation-Laboratory. Rev. Sci. Instruments. 63:1992;1736-1740.
29. Wildegger G., Kiefhaber T. Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 271:1997;294-304.
30. Wu L. C., Peng Z.-Y., Kim P. S. Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2:1995;281-286.