Structural studies of hen egg-white lysozyme dimer: Comparison with monomer

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 7-8, 2008, Pages 1043-1049

  Maroufi, Bahman ^a   Ranjbar, Bijan ^a   Khajeh, Khosro ^a   Naderi Manesh, Hossein ^a   Yaghoubi, Hashem ^a  

^a TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

Equilibrium unfolding; Intermediate; Lysozyme dimer; Mass spectrometry; Thermal unfolding

Indexed keywords

DIMER; EGG WHITE; GADOLINIUM CHLORIDE; LYSOZYME; MONOMER;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CROSS LINKING; ENZYME ACTIVITY; ENZYME MECHANISM; HEN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMODYNAMICS;

ANIMALS; CHROMATOGRAPHY, LIQUID; CIRCULAR DICHROISM; DIMERIZATION; EGG PROTEINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MURAMIDASE; PROTEIN DENATURATION; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 52449135498     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.03.010     Document Type: Article

References (37)

1. Kim P.S., and Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59 (1990) 631-660
2. Arai M., and Kuwajima K. Role of the molten globule state in protein folding. Adv. Protein Chem. 53 (2000) 209-282
3. Chamberlain A.K., and Marqusee S. Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms. Adv. Protein Chem. 53 (2000) 283-328
4. Dill K.A., and Shortle D. Denatured states of proteins. Annu. Rev. Biochem. 60 (1991) 795-825
5. Creighton T.E., Darby N.J., and Kemmink J. The roles of partly folded intermediates in protein folding. FASEB J. 10 (1996) 110-118
6. Roder H., and Colon W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7 (1997) 15-28
7. Shakhnovich E.I. Theoretical studies of protein folding thermodynamics and kinetics. Curr. Opin. Struct. Biol. 7 (1997) 29-40
8. Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-229
9. Dill K., and Chan H. From Levinthal to pathways to funnels. Nature Struct. Biol. 4 (1997) 10-19
10. Fink A.L., Oberg K.A., and Seshadri S. Discrete intermediate versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin. Folding Des. 3 (1998) 19-25
11. Hosseinkhani S., Ranjbar B., Naderi-Manesh H., and Nemat-Gorgani M. Chemical modification of glucose oxidase: possible formation of molten globule-like intermediate structure. FEBS Lett. 561 (2004) 213-216
12. Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24 (1970) 1-95
13. Dobson C.M., Evans P.A., and Radford S.E. Understanding how proteins fold: the lysozyme story so far. Trends Biochem. Sci. 19 (1994) 31-37
14. Haezebrouck P., Joniau M., Van Dael H., Hooke S.D., Woodruff N.D., and Dobson C.M. An equilibrium partially folded state of human lysozyme at low pH. J. Mol. Biol. 246 (1995) 382-387
15. Chen L., Hodgson K.O., and Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261 (1996) 658-671
16. Sasahara K., Demura M., and Nitta K. Partially unfolded equilibrium state of hen lysozyme studied by circular dichroism spectroscopy. Biochemistry 39 (2000) 6475-6482
17. Hameed M., Ahmad B., Fazili K.M., Andrabi K., and Khan R.H. Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol. J. Biochem. (Tokyo) 141 (2007) 573-583
18. Follmer C., and Carlini C.R. Effect of chemical modification of histidines on the copper-induced oligomerization of jack bean urease (EC 3.5.1.5). Arch. Biochem. Biophys. 435 (2005) 15-20
19. Guixé V. Chemical modification of SH groups of E. coli phosphofructokinase-2 induces subunit dissociation: monomers are inactive but preserve ligand binding properties. Arch. Biochem. Biophys. 376 (2000) 313-319
20. Lu Q. Seamless cloning and gene fusion. Trends Biotechnol. 23 (2005) 199-207
21. Hassani L., Ranjbar B., Khajeh K., Naderi-Manesh H., Naderi-Manesh M., and Sadeghi M. Horseradish peroxidase thermostabilization: the combinatorial effects of the surface modification and the polyols. Enzyme Microb. Technol. 38 (2006) 118-125
22. Fancy D.A. Elucidation of protein-protein interactions using chemical cross-linking or label transfer techniques. Curr. Opin. Chem. Biol. 4 (2000) 28-33
23. Phizicky E.M., and Fields S. Protein-protein interactions: methods for detection and analysis. Microbiol. Rev. 59 (1995) 94-123
24. Lundblad R. Cross-linking of proteins. Techniques in protein modification (1994), CRC Press 249-252
25. Simons B.L., King M.C., Cyr T., Hefford M.A., and Kaplan H. Covalent cross-linking of proteins without chemical reagents. Protein Sci. 11 (2002) 1558-1564
26. Simons B.L., Kaplan H., and Hefford M.A. Novel cross-linked enzyme-antibody conjugates for Western blot and ELISA. J. Immunol. Methods 315 (2006) 88-98
27. Sasahara K., Demura M., and Nitta K. Equilibrium and kinetic folding of hen egg-white lysozyme under acidic conditions. Proteins 49 (2002) 472-482
28. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
29. Shugar D. The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme. Biochim. Biophys. Acta 8 (1952) 302-309
30. Nozaki Y. The preparation of guanidine hydrochloride. Methods Enzymol. 26 (1972) 43-50
31. Yaghoubi H., Khajeh K., Hosseinkhani S., Ranjbar B., and Naderi-Manesh H. Application of zero-length cross-linking to form lysozyme, horseradish peroxidase and lysozyme-peroxidase dimers: activity and stability. Int. J. Biol. Macromol. 41 (2007) 624-630
32. Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
33. Tanford C. Protein denaturation. Adv. Protein Chem. 23 (1968) 121-282
34. Aune K.C., and Tanford C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25 degrees. Biochemistry 8 (1969) 4586-4590
35. Privalov P.L., and Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86 (1974) 665-684
36. Griko Y.V., Freire E., Privalov G., Van Dael H., and Privalov P.L. The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme. J. Mol. Biol. 252 (1995) 447-459
37. Robson B., and Pain R.H. The mechanism of folding of globular proteins. Equilibria and kinetics of conformational transitions of penicillinase from Staphylococcus aureus involving a state of intermediate conformation. Biochem. J. 155 (1976) 331-344