Strategies for folding of affinity tagged proteins using GroEL and osmolytes

Obtaining a proper fold of affinity tagged chimera proteins can be difficult. Frequently, the protein of interest aggregates after the chimeric affinity tag is cleaved off, even when the entire chimeric construct is initially soluble. If the attached protein is incorrectly folded, chaperone proteins...

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Bibliographic Details
Published in:	Journal of structural and functional genomics Vol. 10; no. 1; pp. 57 - 66
Main Authors:	Katayama, Hiroo, McGill, Mitchell, Kearns, Andrew, Brzozowski, Marek, Degner, Nicholas, Harnett, Bliss, Kornilayev, Boris, Matković-Čalogović, Dubravka, Holyoak, Todd, Calvet, James P, Gogol, Edward P, Seed, John, Fisher, Mark T
Format:	Journal Article
Language:	English
Published:	Dordrecht Dordrecht : Springer Netherlands 01-03-2009 Springer Netherlands Springer Nature B.V
Subjects:	Binding Sites Biochemistry Bioinformatics Biomedical and Life Sciences Cells, Cultured Chaperonin 60 - chemistry Chaperonin 60 - genetics Chaperonin 60 - metabolism Chaperonins - chemistry Chaperonins - metabolism Dehydrogenases E coli Experiments Forestry Management Human Genetics Humans Life Sciences Microbial Genetics and Genomics Models, Molecular Phosphoenolpyruvate Carboxykinase (ATP) - chemistry Phosphoenolpyruvate Carboxykinase (ATP) - metabolism Plant Genetics and Genomics Plasmids Protein Conformation Protein Folding Proteomics - methods Recombinant Fusion Proteins - chemistry Time Factors Chaperonin Protein stability Affinity tags Protein folding Osmolytes
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