Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism

Biochemistry

Volumn 44, Issue 17, 2005, Pages 6685-6692

  Nakao, Masaharu ^a   Maki, Kosuke ^a   Arai, Munehito ^b   Koshiba, Takumi ^c,d   Nitta, Katsutoshi ^c   Kuwajima, Kunihiro ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c HOKKAIDO UNIVERSITY   (Japan)

^d CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; EXCITONS; PROTEINS; REACTION KINETICS; SPECTROSCOPIC ANALYSIS;

BURST-PHASE INTERMEDIATES; CANINE MILK LYSOZYME; KINETIC FOLDING INTERMEDIATES; STOPPED-FLOW MEASUREMENTS;

BIOCHEMISTRY;

CALCIUM BINDING PROTEIN; CANINE MILK LYSOZYME; RECOMBINANT ENZYME; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN PROCESSING; STRUCTURAL PROTEOMICS; STRUCTURE ANALYSIS;

ANIMALS; CIRCULAR DICHROISM; DOGS; GUANIDINE; HEAT; KINETICS; MILK PROTEINS; MODELS, CHEMICAL; MODELS, MOLECULAR; MURAMIDASE; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; TRYPTOPHAN;

EID: 17844392322     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050082+     Document Type: Article

References (27)

1. Kim, P. S., and Baldwin, R. L. (1990) Intermediates in the folding reactions of small proteins, Annu. Rev. Biochem. 59, 631-660.
2. Arai, M., and Kuwajima, K. (1996) Rapid formation of a molten globule intermediate in refolding of á-lactalbumin, Folding Des. 1, 275-287.
3. Ptitsyn, O. B. (1987) Protein folding: Hypothesis and experiments, J. Protein Chem. 6, 273-293.
4. Kuwajima, K. (1989) The molten globule state as a clue of understanding the folding and cooperativity of globular-protein structure, Proteins 6, 87-103.
5. Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E., and Razgulyaev, O. I. (1990) Evidence for a molten globule state as a general intermediate in protein folding, FEBS Lett. 262, 20-24.
6. Koshiba, T., Yao, M., Kobashigawa, Y., Demura, M., Nakagawa, A., Tanaka, I., Kuwajima, K., and Nitta, K. (2000) Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme, Biochemistry 39, 3248-3257.
7. Kobashigawa, Y., Demura, M., Koshiba, T., Kumaki, Y., Kuwajima, K., and Nitta, K. (2000) Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule, Proteins 40, 579-589.
8. Nakao, M., Arai, M., Koshiba, T., Nitta, K., and Kuwajima, K. (2003) Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy, Spectroscopy 17, 183-193.
9. Mizuguchi, M., Arai, M., Ke, Y., Nitta, K., and Kuwajima K. (1998) Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy, J. Mol. Biol. 283, 265-277.
10. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-280.
11. Kikuchi, M., Kawano, K., and Nitta, K. (1998) Calcium-binding and structural stability of echidna and canine milk lysozyme, Protein Sci. 7, 2150-2155.
12. 2+-induced alteration in the unfolding behavior of α-lactalbumin, J. Biochem. 99, 1191-1201.
13. Kuwajima, K., Garvey, E. P., Finn, B. E., Matthews, C. R., and Sugai, S. (1991) Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy, Biochemistry 30, 7693-7703.
14. Woody, R. W., and Dunker, A. K. (1996) Aromatic and cystine side-chain CD in proteins, Circular Dichroism and the Conformational Analysis of Biomolecules, pp 109-157, Plenum Press, New York.
15. Morozova-Roche, L. A., Jones, J. A., Noppe, W., and Dobson, C. M. (1999) Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme, J. Mol. Biol. 289, 1055-1073.
16. Morozova-Roche, L. A., Arico-Muendel, C. C., Haynie, D. T., Emelyanenko, V. I., Van Dael, H., and Dobson, C. M. (1997) Structural characterisation and comparison of the native and A-states of equine lysozyme, J. Mol. Biol. 268, 903-921.
17. Van Dael, H., Haezebrouck, P., and Joniau, M. (2003) Equilibrium and kinetic studies on folding of canine milk lysozyme, Protein Sci. 12, 609-619.
18. Chaudhuri, T. K., Horii, K., Yoda, T., Arai, M., Nagata, S., Terada, T. P., Uchiyama, H., Ikura, T., Tsumoto, K., Kataoka, H., Matsushima, M., Kuwajima, K., and Kumagai, I. (1999) Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli, J. Mol. Biol. 285, 1179-1194.
19. Chaudhuri, T. K., Arai, M., Terada, T. P., Ikura, T., and Kuwajima, K. (2000) Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy, Biochemistry 39, 15643-15651.
20. Jamin, M., and Baldwin, R. L. (1998) Two forms of the pH 4 folding intermediate of apomyoglobin, J. Mol. Biol. 276, 491-504.
21. Matagne, A., and Dobson, C. M. (1998) The folding process of hen lysozyme: A perspective from the 'new view', Cell. Mol. Life Sci. 54, 363-371.
22. Segel, D. J., Bachmann, A., Hofrichter, J., Hodgson, K. O., Doniach, S., and Kiefhaber, T. (1999) Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scatterin, J. Mol. Biol. 288, 489-499.
23. Gladwin, S. T., and Evans, P. A. (1996) Structure of very early protein folding intermediates: New insights through a variant of hydrogen exchange labeling, Folding Des. 1, 407-417.
24. Arai, M., and Kuwajima, K. (2000) The role of the molten globule state in protein folding, Adv. Protein Chem. 53, 209-282.
25. Kuwajima, K., and Arai, M. (2000) The molten globule state: The physical picture and biological significance, in Mechanisms of Protein Folding (Pain, R. H., Ed.) 2nd ed., pp 138-174, Oxford University Press, New York.
26. Kamagata, K., Arai, M., and Kuwajima, K. (2004) Unification of the folding mechanisms of non-two-state and two-state proteins, J. Mol. Biol. 339, 951-965.
27. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.