Unfolding kinetics of dimeric creatine kinase measured by stopped-flow small angle X-ray scattering

Biochimie

Volumn 86, Issue 2, 2004, Pages 127-132

  Zhu, Li ^a   Qin, Zhi Jie ^a,b   Zhou, Jun Mei ^a   Kihara, Hiroshi ^b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b KANSAI MEDICAL UNIVERSITY   (Japan)

Author keywords

ME; mercaptoethanol; CK; Creatine kinase; Guanidine hydrochloride; GuHCl; Monophasic kinetics; Protein folding; SAXS; Small angle X ray scattering; Urea

Indexed keywords

CREATINE KINASE; GLYCEROL; GUANIDINE; UREA;

APPARATUS; ARTICLE; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); ENZYME DENATURATION; ENZYME KINETICS; FLUORESCENCE; INTERMETHOD COMPARISON; MEASUREMENT; PROTEIN FOLDING; PROTEIN STRUCTURE; SPECTROSCOPY; STRUCTURE ANALYSIS; SYNCHROTRON RADIATION; TIME; X RAY CRYSTALLOGRAPHY;

CIRCULAR DICHROISM; CREATINE KINASE; DIMERIZATION; KINETICS; PROTEIN DENATURATION; PROTEIN FOLDING; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE; SYNCHROTRONS; TIME FACTORS; UREA; X-RAYS;

EID: 1542358056     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2003.12.002     Document Type: Article

References (17)

1. Glatter O., Kratky O. Small Angle X-ray Scattering. 1982;Academic Press, London.
2. Lattman E.E. Small angle scattering studies of protein folding. Curr. Opin. Struct. Biol. 4:1994;87-92.
3. Doniach S. Changes in biomolecular conformation seen by small angle X-ray scattering. Chem. Rev. 101:2001;1763-1778.
4. Kataoka M., Nishii I., Fujisawa T., Ueki T., Tokunaga F., Goto Y. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249:1995;215-228.
5. Semisotnov G.V., Kihara H., Kotova N.V., Kimura K., Amemiya Y., Wakabayashi K., Serdyuk I.N., Timchenko A.A., Chiba K., Nikaido K., Ikura T., Kuwajima K. Protein globularization during folding: a study by synchrotron small-angle X-ray scattering. J. Mol. Biol. 262:1996;559-574.
6. Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., Belagaje R., Biemann K., Page D., Kuby S., Schimmel P. Rabbit muscle creatine phosphokinase. J. Biol. Chem. 259:1984;14317-14320.
7. Kihara H. Stopped-flow apparatus for X-ray scattering and XAFS. J. Synchrotron Rad. 1:1994;74-77.
8. Yao Q.Z., Hou L.X., Zhou H.M., Tsou C.L. Conformational changes of creatine kinase during guanidine hydrochloride denaturation. Sci. Sin. (Engl. Ed.). 25B:1982;1186-1193.
9. Noda L., Kuby S., Lardy H. ATP-creatine transphosphorylase. Methods Enzymol. 2:1955;605-610.
10. Mahowald T.A., Noltmann E.A., Kuby S.A. Studies on adenosine triphosphate transphosphorylases. J. Biol. Chem. 237:1962;1535-1548.
11. Amemiya Y., Wakabayashi K., Hamanaka T., Wakabayashi T., Hashizume H. Design of a small-angle X-ray diffractometer using synchrotron radiation at the photon factory. Nucl. Instrum. Methods. 208:1983;471-477.
12. Fan Y.X., Zhou J.M., Kihara H., Tsou C.L. Unfolding and refolding of dimeric creatine kinase: equilibrium and kinetic studies. Protein Sci. 7:1998;2631-2641.
13. Zhu L., Fan Y.X., Perrett S., Zhou J.M. Relationship between kinetic and equilibrium folding intermediates of creatine kinase. Biochem. Biophys. Res. Commun. 285:2001;857-862.
14. Kuznetsovaa I.M., Stepanenko O.V., Turoverova K.K., Zhu L., Zhou J.M., Fink A.L., Uversky V.N. Unraveling multistate unfolding of rabbit muscle creatine kinase. Biochim. Biophys. Acta. 1596:2002;138-155.
15. Zhou J.M., Fan Y.X., Kihara H., Kimura K., Amemiya Y. Unfolding of dimeric creatine kinase in urea and guanidine hydrochloride as measured using small angle X-ray scattering with synchrotron radiation. FEBS Lett. 415:1997;183-185.
16. Zhu L., Fan Y.X., Zhou J.M. Identification of equilibrium and kinetic intermediates involved in folding of urea-denatured creatine kinase. Biochim. Biophys. Acta. 1544:2001;320-332.
17. Plaxco K.W., Millett I.S., Segel D.J., Doniach S., Baker D. Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nat. Struct. Biol. 6:1999;554-556.