Unfolding and aggregation-associated changes in the secondary structure of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride as monitored by FTIR

Biospectroscopy

Volumn 3, Issue 2, 1997, Pages 121-129

  Li, Xiao Feng ^a   Zhou, Jun Mei ^a  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Aggregated state; D glyceraldehyde 3 phosphate dehydrogenase; Folding and unfolding; FTIR spectroscopy; Guanidine denaturation

Indexed keywords

EID: 0001179028     PISSN: 10754261     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1520-6343(1997)3:2<121::aid-bspy5>3.0.co;2-a     Document Type: Article

References (26)

1. G. Zettlmeissl, R. Rudolph, and R. Jaenicke, "Reconstitution of lactic dehydrogenase: Noncovalent aggregation vs. reaction: 1. Physical properties and kinetics of aggregation," Biochemistry, 18, 5567-5571 (1979).
2. J. London, C. Skrzynia, and M. Goldberg, "Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea," Eur. J. Biochem., 47, 409-415 (1974).
3. D. Goldenberg and J. King, "Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22," Proc. Natl. Acad. Sci. USA, 79, 3403-3407 (1982).
4. H. H. Bauer, M. Muller, J. Goette, H. P. Merkle, and U. P. Fringeli, "Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FTIR spectroscopy," Biochemistry, 33, 12276-12282 (1994).
5. J. H. Fuhrhop, M. Krull, and G. Buldt, "Precipitates with β-pleated sheet structure by mixing aqueous solution of helical poly(D-lysine) and poly(L-lysine)," Angew. Chem. Int. Ed. Eng., 26, 699-700 (1987).
6. K. Oberg, B. A. Chrunky, R. Wetzel, and A. L. Fink, "Nativelike secondary structure in interleukin-1β inclusion bodies by attenuated total reflectance FTIR," Biochemistry, 33, 2628-2634 (1994).
7. Y. S. He and C. L. Tsou, "Formation of a new fluorophore on irradiation of carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase," Nature, 277, 245-246 (1979).
8. G. F. Xie and C. L. Tsou, "Conformational and activity changes during guanidine denaturation of D-glyceraldehyde-3-phosphate dehydrogenase," Biochim. Biophys. Acta, 911, 19-24 (1987).
9. Y. Z. Lin, S. J. Liang, J. M. Zhou, C. L. Tsou, P. Q. Wu, and Z. K. Zhou, "Comparison of inactivation and conformational changes of D-glyceraldehyde-3-phosphate dehydrogenase during thermal denaturation," Biochim. Biophys. Acta, 1038, 247-252 (1990).
10. Z. J. Lin, J. Li, F. M. Zhang, S. Y. Song, J. Yang, S. J. Liang, and C. L. Tsou, "Structure of D-glyceraldehyde-3-phosphate dehydrogenase from palinurus versicolor carrying the fluorescent NAD derivatives at 2.7 A resolution," Arch. Biochim. Biophys., 302, 161-166 (1993).
11. S. J. Liang, Y. Z. Lin, J. M. Zhou, C. L. Tsou, P. Q. Wu, and Z. K. Zhou, "Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride," Biochim. Biophys. Acta, 1038, 240-246 (1990).
12. W. S. Allison and N. O. Kaplan, "The comparative enzymology of triosephosphate dehydrogenase," J. Biol. Chem., 239, 2140-2152 (1964).
13. Y. S. Ho, Y. N. Lien, S. H. Chiang, and C. L. Tsou, "Formation of a new fluorophore on irradiation of carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase," Sicentia Sinica, 22, 207-221 (1979).
14. A. Dong, P. Huang, and W. S. Caughey, "Protein secondary structures in water from second-derivative amide I infrared spectra," Biochemistry, 29, 3303-3308 (1990).
15. M. Buehner, G. C. Ford, D. Moras, K. W. Olsen, and M. G. Rossmann, "Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase," J. Mol. Biol., 90, 25-49 (1974).
16. B. E. Bowler, K. May, T. Zaragoza, P. York, A. Dong, and W. S. Caughey, "Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids," Biochemistry, 32, 183-190 (1993).
17. B. E. Bowler, A. Dong, and W. S. Caughey, "Characterization of the guanidine hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy," Biochemistry, 33, 2402-2408 (1994).
18. D. W. Darnall and T. D. Barela, "β-Structure in glyceraldehyde-3-phosphate dehydrogenase," Biochim. Biophys. Acta, 236, 593-598 (1971).
19. N. Nemoto, T. Kiyohara, Y. Tsuanshima, and M. Kurata, "Raman, IR and CD spectroscopy on aggregates and gels of lysozyme in alcohols," Bull. Inst. Chem. Res. (Kyoto), 61, 203-213 (1983).
20. V. J. C. Lin and J. L. Koenig, "Raman studies of bovine serum albumin," Biopolymers, 15, 203-218 (1976).
21. P. C. Painter and J. L. Koenig, "Raman spectroscopic study of the proteins of egg white," Biopolymers, 15, 2155-2166 (1976).
22. S. N. Timasheff and L. Stevens, "Infrared spectra and protein conformations in aqueous solution," J. Biol. Chem., 242, 5467-5473 (1967).
23. T. T. Herskovits, B. Gadegbeku, and H. Jaillet, "On the structural stability and solvent denaturation of proteins," J. Biol. Chem., 245, 2588-2598 (1970).
24. D. B. Wetlaufer and Y. Xie, "Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II," Protein Sci., 4, 1535-1543 (1995).
25. H. Fabian, C. Schultz, D. Naumann, O. Landt, U. Hahn, and W. Saenger, "Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study," J. Mol. Biol., 232, 967-981 (1993).
26. J. L. R. Arrindo, N. M. Young, and H. H. Mantsch, "The solution structure of concanavalin A probed by FT-IR spectroscopy," Biochim. Biophys. Acta, 952, 261-268 (1988).