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Confirmation of TDP1–PARP1 direct binding using SPR. (A) Representative concentration-dependent binding of TDP1 to immobilized PARP1 on a <t>CM5</t> chip surface. Colored lines are experimental data and dashed lines are fit to a 1 : 1 binding model. The association rate constant ( k a ), dissociation rate constant ( k d ), and equilibrium dissociation constant ( K D , affinity) were determined from three independent set of analyte injections. (B) SPR sensorgrams showing lack of direct binding of TDP1 to immobilized control protein, GST, on the CM5 chip surface.
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Confirmation of TDP1–PARP1 direct binding using SPR. (A) Representative concentration-dependent binding of TDP1 to immobilized PARP1 on a <t>CM5</t> chip surface. Colored lines are experimental data and dashed lines are fit to a 1 : 1 binding model. The association rate constant ( k a ), dissociation rate constant ( k d ), and equilibrium dissociation constant ( K D , affinity) were determined from three independent set of analyte injections. (B) SPR sensorgrams showing lack of direct binding of TDP1 to immobilized control protein, GST, on the CM5 chip surface.
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Confirmation of TDP1–PARP1 direct binding using SPR. (A) Representative concentration-dependent binding of TDP1 to immobilized PARP1 on a <t>CM5</t> chip surface. Colored lines are experimental data and dashed lines are fit to a 1 : 1 binding model. The association rate constant ( k a ), dissociation rate constant ( k d ), and equilibrium dissociation constant ( K D , affinity) were determined from three independent set of analyte injections. (B) SPR sensorgrams showing lack of direct binding of TDP1 to immobilized control protein, GST, on the CM5 chip surface.
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Confirmation of TDP1–PARP1 direct binding using SPR. (A) Representative concentration-dependent binding of TDP1 to immobilized PARP1 on a <t>CM5</t> chip surface. Colored lines are experimental data and dashed lines are fit to a 1 : 1 binding model. The association rate constant ( k a ), dissociation rate constant ( k d ), and equilibrium dissociation constant ( K D , affinity) were determined from three independent set of analyte injections. (B) SPR sensorgrams showing lack of direct binding of TDP1 to immobilized control protein, GST, on the CM5 chip surface.
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Confirmation of TDP1–PARP1 direct binding using SPR. (A) Representative concentration-dependent binding of TDP1 to immobilized PARP1 on a CM5 chip surface. Colored lines are experimental data and dashed lines are fit to a 1 : 1 binding model. The association rate constant ( k a ), dissociation rate constant ( k d ), and equilibrium dissociation constant ( K D , affinity) were determined from three independent set of analyte injections. (B) SPR sensorgrams showing lack of direct binding of TDP1 to immobilized control protein, GST, on the CM5 chip surface.

Journal: Physical Chemistry Chemical Physics

Article Title: Identifying potential binding sites for complex formation between Tyrosyl-DNA phosphodiesterase 1 and poly [ADP-ribose] polymerase 1

doi: 10.1039/d6cp00941g

Figure Lengend Snippet: Confirmation of TDP1–PARP1 direct binding using SPR. (A) Representative concentration-dependent binding of TDP1 to immobilized PARP1 on a CM5 chip surface. Colored lines are experimental data and dashed lines are fit to a 1 : 1 binding model. The association rate constant ( k a ), dissociation rate constant ( k d ), and equilibrium dissociation constant ( K D , affinity) were determined from three independent set of analyte injections. (B) SPR sensorgrams showing lack of direct binding of TDP1 to immobilized control protein, GST, on the CM5 chip surface.

Article Snippet: SPR measurements were carried out using a Biacore T200 instrument with CM5 chips at 25 °C.

Techniques: Binding Assay, Concentration Assay, Control