nonlinear regression curve fit analysis model Search Results


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OriginLab corp nonlinear regression model curve
Expected outcomes of the Fluorescence polarized assay of mVDAC1 (A) Binding of the NADH (at 5 μM) to increasing concentrations of mVDAC1 measured by fluorescence polarization (FP). The dissociation constant (KD) obtained by fitting the fluorescence polarization values and the protein concentrations into a <t>nonlinear</t> <t>regression</t> <t>model</t> <t>curve</t> in Origin Lab is about 7 μM. (B) Displacement curves of the NADH (5 μM) from mVDAC1 with increased concentrations of small-molecule D10. The molecule can compete with NADH binding with an apparent KD in the micromolar range (KD = 18.5 ± 0.2). Data are expressed as mean ± SEM ( n = 3). Reproduced from.
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GraphPad Software Inc nonlinear regression model fit with settings for log agonist/inhibitor versus normalized response curves
Expected outcomes of the Fluorescence polarized assay of mVDAC1 (A) Binding of the NADH (at 5 μM) to increasing concentrations of mVDAC1 measured by fluorescence polarization (FP). The dissociation constant (KD) obtained by fitting the fluorescence polarization values and the protein concentrations into a <t>nonlinear</t> <t>regression</t> <t>model</t> <t>curve</t> in Origin Lab is about 7 μM. (B) Displacement curves of the NADH (5 μM) from mVDAC1 with increased concentrations of small-molecule D10. The molecule can compete with NADH binding with an apparent KD in the micromolar range (KD = 18.5 ± 0.2). Data are expressed as mean ± SEM ( n = 3). Reproduced from.
Nonlinear Regression Model Fit With Settings For Log Agonist/Inhibitor Versus Normalized Response Curves, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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GraphPad Software Inc fitting models to biological data using linear and nonlinear regression, a practical guide to curve fitting
Expected outcomes of the Fluorescence polarized assay of mVDAC1 (A) Binding of the NADH (at 5 μM) to increasing concentrations of mVDAC1 measured by fluorescence polarization (FP). The dissociation constant (KD) obtained by fitting the fluorescence polarization values and the protein concentrations into a <t>nonlinear</t> <t>regression</t> <t>model</t> <t>curve</t> in Origin Lab is about 7 μM. (B) Displacement curves of the NADH (5 μM) from mVDAC1 with increased concentrations of small-molecule D10. The molecule can compete with NADH binding with an apparent KD in the micromolar range (KD = 18.5 ± 0.2). Data are expressed as mean ± SEM ( n = 3). Reproduced from.
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Expected outcomes of the Fluorescence polarized assay of mVDAC1 (A) Binding of the NADH (at 5 μM) to increasing concentrations of mVDAC1 measured by fluorescence polarization (FP). The dissociation constant (KD) obtained by fitting the fluorescence polarization values and the protein concentrations into a nonlinear regression model curve in Origin Lab is about 7 μM. (B) Displacement curves of the NADH (5 μM) from mVDAC1 with increased concentrations of small-molecule D10. The molecule can compete with NADH binding with an apparent KD in the micromolar range (KD = 18.5 ± 0.2). Data are expressed as mean ± SEM ( n = 3). Reproduced from.

Journal: STAR Protocols

Article Title: Protocol for high-yield bacterial expression and purification of the voltage-dependent anion channel 1 for high-throughput biophysical assays

doi: 10.1016/j.xpro.2024.103557

Figure Lengend Snippet: Expected outcomes of the Fluorescence polarized assay of mVDAC1 (A) Binding of the NADH (at 5 μM) to increasing concentrations of mVDAC1 measured by fluorescence polarization (FP). The dissociation constant (KD) obtained by fitting the fluorescence polarization values and the protein concentrations into a nonlinear regression model curve in Origin Lab is about 7 μM. (B) Displacement curves of the NADH (5 μM) from mVDAC1 with increased concentrations of small-molecule D10. The molecule can compete with NADH binding with an apparent KD in the micromolar range (KD = 18.5 ± 0.2). Data are expressed as mean ± SEM ( n = 3). Reproduced from.

Article Snippet: The dissociation constant (KD) obtained by fitting the fluorescence polarization values and the protein concentrations into a nonlinear regression model curve in Origin Lab is about 7 μM. (B) Displacement curves of the NADH (5 μM) from mVDAC1 with increased concentrations of small-molecule D10.

Techniques: Fluorescence, Binding Assay