Panel A shows the pressure FRET ratio baseline data (open circle) and polynomial smoothing curve (solid line for oligonucleotide A

Copyright information:Taken from "Pressure dissociation of integration host factor–DNA complexes reveals flexibility-dependent structural variation at the protein–DNA interface"Nucleic Acids Research 2007;35(6):1761-1772.Published online 25 Feb 2007PMCID:PMC1874591.© 2007 The Author(s)6 in...

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Hauptverfasser: Senear, Donald F., Tretyachenko-Ladokhina, Vira, Opel, Michael L., Aeling, Kimberly A., G. Wesley Hatfield, Franklin, Laurie M., Darlington, Reuben C., J.B. Alexander Ross
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Zusammenfassung:Copyright information:Taken from "Pressure dissociation of integration host factor–DNA complexes reveals flexibility-dependent structural variation at the protein–DNA interface"Nucleic Acids Research 2007;35(6):1761-1772.Published online 25 Feb 2007PMCID:PMC1874591.© 2007 The Author(s)6 in the absence of IHF compared with unprocessed data for 10 nM DNA and 25 nM IHF (filled square) (10 mM Tris pH 8.0, 100 mM NaCl and 1 mM EDTA). Panel B compares fraction bound for oligonucleotides A.2 (filled diamond) and A.6 (filled square) at 10 nM DNA, 25 nM IHF, i.e. same A.6 data as panel A and same reaction conditions. Solid and dashed curves are the fits and 95% confidence intervals to these individual experiments, using equations () as described in the text.
DOI:10.6084/m9.figshare.55507