Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates

The chaperonin GroEL of the heat shock protein family from Escherichia coli cells can bind various polypeptides lacking rigid tertiary structure and thus prevent their nonspecific association and provide for acquisition of native conformation. In the present work we studied the interaction of GroEL...

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Veröffentlicht in:	Biochemistry (Moscow) 2006-12, Vol.71 (12), p.1357-1364
Hauptverfasser:	Marchenko, N Iu, Marchenkov, V V, Kaĭsheva, A L, Kashparov, I A, Kotova, N V, Kaliman, P A, Semisotnov, G V
Format:	Artikel
Sprache:	eng
Schlagworte:	Anisotropy Calcium - chemistry Cations Cations, Divalent - chemistry Chaperonins - chemistry Chaperonins - isolation & purification Chromatography, Affinity E coli Escherichia coli Escherichia coli - chemistry Escherichia coli Proteins - chemistry Escherichia coli Proteins - isolation & purification Fluorescence Heat-Shock Proteins - chemistry Heat-Shock Proteins - isolation & purification Hydrophobic and Hydrophilic Interactions Magnesium - chemistry Osmolar Concentration Protein Denaturation Protein folding Proteins Static Electricity
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