Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins

Biophysical Chemistry

Volumn 101-102, Issue , 2002, Pages 133-144

  Kalnine, N N ^a   Schachman, H K ^b  

^a BD BIOSCIENCES   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Analysis of patterns by mass transfer equations; Aspartate transcarbamoylase and catalytic trimers; Denaturation and reconsitution of oligomeric proteins; Unfolding and folding of polypeptide chains; Urea gradient gel electrophoresis

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; OLIGOMER; POLYPEPTIDE; LIGAND; PROTEIN; UREA;

ARTICLE; CATALYSIS; CATALYST; CONCENTRATION RESPONSE; DISSOCIATION; ENZYME SUBUNIT; GEL ELECTROPHORESIS; KINETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; QUANTITATIVE ANALYSIS; REPRODUCIBILITY; STAINING; BINDING SITE; CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS;

BINDING SITES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; KINETICS; LIGANDS; PROTEINS; REPRODUCIBILITY OF RESULTS; UREA;

EID: 18744380634     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00154-0     Document Type: Article

References (24)

1. Kuwajima K. Protein folding in vitro. Curr. Opin. Biotechnol. 3:1992;462-467.
2. Hamada D., Segawa S., Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nat. Struct. Biol. 3:1996;868-873.
3. Udgaonkar J., Baldwin R. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 335:1988;694-699.
4. Kalnin N.N., Kuwajima K. Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped-flow circular dichroism. Proteins. 23:1995;163-176.
5. Chamberlain A.K., Handel T.M., Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RnaseH. Nat. Struct. Biol. 3:1996;782-787.
6. Dill K., Chan H. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:1997;10-18.
7. Milla M., Brown B., Waldburger C., Sauer R. P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry. 34:1995;13914-13919.
8. Neet K., Timm D. Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci. 3:1994;2167-2174.
9. Herold M., Kirschner K. Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate. Biochemistry. 29:1990;1907-1913.
10. Blond S., Goldberg M. Kinetics and importance of the dimerization step in the folding pathway of the beta 2 subunit of Escherichia coli tryptophan synthase. J. Mol. Biol. 182:1985;597-606.
11. Jaenicke R. Protein folding and association: in vitro studies for self-organization and targeting in the cell. Curr. Top. Cell. Regul. 24:1996;209-214.
12. Creighton T. Electrophoretic analysis of the unfolding of proteins by urea. J. Mol. Biol. 129:1979;235-264.
13. Creighton T. Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J. Mol. Biol. 137:1980;61-80.
14. Burns D., Schachman H. Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains. J. Biol. Chem. 257:1982;8648-8654.
15. Burns D., Schachman H. Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers. J. Biol. Chem. 257:1982;8638-8647.
16. Bromberg S., LiCata V., Mallikarachchi D., Allewell N. Ligation alters the pathway of urea-induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase. Protein Sci. 3:1994;1236-1244.
17. Cann J.R. Interacting macromolecules; the theory and practice of their electrophoresis, ultracentrifugation, and chromatography. 1970;Academic Press, New York.
18. Mitchell R.M. The spatial distribution of moving macromolecules undergoing isomerization. Biopolymers. 15:1976;1717-1739.
19. Janknecht R., de Martynoff G., Lou J., Hipskind R., Nordheim A. Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc. Natl. Acad. Sci. USA. 88:1991;8972-8976.
20. Graf R., Schachman H.K. Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. USA. 93:1996;11591-11596.
21. Yang Y., Kirschner M., Schachman H. Aspartate transcarbamoylase (Escherichia coli): preparation of subunits. Methods Enzymol. 51:1978;35-41.
22. Goldenberg D.P. Creighton T.E. Protein structure: a practical approach. 1997;187-218 Oxford University Press, Inc, New York.
23. M.A. Bothwell, Kinetics and Thermodynamics of Subunit Interactions in Aspartate Transcarbamylase. 1975, Ph.D. thesis in Biochemistry, University of California, Berkeley.
24. Yang Y., Schachman H.K. Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase. Anal. Biochem. 163:1987;188-195.