Thermodynamics of the Interaction of the Escherichia coli Regulatory Protein TyrR with DNA Studied by Fluorescence Spectroscopy

Fluorescence quenching was used to study the site-specific binding of the Escherichia coli regulatory protein TyrR to a fluoresceinated oligonucleotide (9F30A/30B) containing a TyrR binding site. The equilibrium constant for the interaction (K L) was measured as a function of temperature and salt co...

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Veröffentlicht in:	Biochemistry (Easton) 1998-05, Vol.37 (20), p.7431-7443
Hauptverfasser:	Bailey, Michael F, Davidson, Barrie E, Haralambidis, Jim, Kwok, Terry, Sawyer, William H
Format:	Artikel
Sprache:	eng
Schlagworte:	Cations, Monovalent Circular Dichroism DNA, Bacterial - chemistry DNA, Bacterial - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Fluorescein-5-isothiocyanate - metabolism Oligonucleotides - metabolism Protein Binding - genetics Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism Spectrometry, Fluorescence Temperature Thermodynamics
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