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boltzmann sigmoid function in graphpad prism 10  (GraphPad Software Inc)


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    GraphPad Software Inc boltzmann sigmoid function in graphpad prism 10
    Boltzmann Sigmoid Function In Graphpad Prism 10, 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
    https://www.bioz.com/product/boltzmann+sigmoid+function/boltzman+sigmoidal+fit+function+in+graphpad+prism+6+software/pm40327692-251-10-10
    Average 90 stars, based on 1 article reviews
    boltzmann sigmoid function in graphpad prism 10 - by Bioz Stars, 2026-09
    90/100 stars

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    Related Articles

    other:

    Article Title: Computational Stabilization of a Non-Heme Iron Enzyme Enables Efficient Evolution of New Function.
    Article Snippet: Tm values were calculated using the Boltzmann sigmoid function in GraphPad Prism.

    Article Title: Can training of a skilled pelvic movement change corticomotor control of back muscles? Comparison of single and paired-pulse transcranial magnetic stimulation.
    Article Snippet: The three parameters were calculated using the Boltzmann sigmoid function in GraphPad Prism 9 (GraphPad Software Inc., CA, US).

    Software:

    Article Title: Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.
    Article Snippet: .. Data were fitted to a Boltzmann sigmoid function by Prism (GraphPad Software, San Diego, CA) or Protein Thermal ShiftTM Software (ThermoFisher Scientific). ..

    Fluorescence:

    Article Title: Binding of Tetracyclines to Acinetobacter baumannii TetR Involves Two Arginines as Specificity Determinants
    Article Snippet: .. The unfolding temperature ( T m ) was determined by fitting the fluorescence curve to a Boltzmann sigmoid function (GraphPad Prism). ..



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    ( A ) Representative SYPRO Orange thermal unfolding curve of Pro 283 NP, Ser 283 NP, and SYPRO Orange dye with buffer only. Means of four technical replicates are shown with the shaded area representing the SD. ( B ) Circular dichroism spectra of Pro 283 and Ser 283 NP. ( C ) Irreversible T agg was calculated by fitting the plots from (A) to a <t>Boltzmann</t> sigmoidal curve. The experiment was performed at three different NP concentrations. Individual measurements for five technical replicates are shown (**** P < 0.0001). ( D ) Schematic for a cellular thermal shift assay experiment. Intact cells ectopically expressing NP are harvested, split into aliquots, and heated rapidly to the indicated temperatures in a thermocycler. After centrifugation to pellet protein aggregates, soluble NP remaining in the supernatant is quantified via immunoblot. ( E ) Quantification of cellular thermal shift assay immunoblots. The mean of biological triplicates is shown with the error bars representing the SD (* P < 0.05). All band intensities were normalized to 37°C. Original blots are shown in fig. S2.
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    ( A ) Representative SYPRO Orange thermal unfolding curve of Pro 283 NP, Ser 283 NP, and SYPRO Orange dye with buffer only. Means of four technical replicates are shown with the shaded area representing the SD. ( B ) Circular dichroism spectra of Pro 283 and Ser 283 NP. ( C ) Irreversible T agg was calculated by fitting the plots from (A) to a Boltzmann sigmoidal curve. The experiment was performed at three different NP concentrations. Individual measurements for five technical replicates are shown (**** P < 0.0001). ( D ) Schematic for a cellular thermal shift assay experiment. Intact cells ectopically expressing NP are harvested, split into aliquots, and heated rapidly to the indicated temperatures in a thermocycler. After centrifugation to pellet protein aggregates, soluble NP remaining in the supernatant is quantified via immunoblot. ( E ) Quantification of cellular thermal shift assay immunoblots. The mean of biological triplicates is shown with the error bars representing the SD (* P < 0.05). All band intensities were normalized to 37°C. Original blots are shown in fig. S2.

    Journal: Science Advances

    Article Title: The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure

    doi: 10.1126/sciadv.adl6144

    Figure Lengend Snippet: ( A ) Representative SYPRO Orange thermal unfolding curve of Pro 283 NP, Ser 283 NP, and SYPRO Orange dye with buffer only. Means of four technical replicates are shown with the shaded area representing the SD. ( B ) Circular dichroism spectra of Pro 283 and Ser 283 NP. ( C ) Irreversible T agg was calculated by fitting the plots from (A) to a Boltzmann sigmoidal curve. The experiment was performed at three different NP concentrations. Individual measurements for five technical replicates are shown (**** P < 0.0001). ( D ) Schematic for a cellular thermal shift assay experiment. Intact cells ectopically expressing NP are harvested, split into aliquots, and heated rapidly to the indicated temperatures in a thermocycler. After centrifugation to pellet protein aggregates, soluble NP remaining in the supernatant is quantified via immunoblot. ( E ) Quantification of cellular thermal shift assay immunoblots. The mean of biological triplicates is shown with the error bars representing the SD (* P < 0.05). All band intensities were normalized to 37°C. Original blots are shown in fig. S2.

    Article Snippet: For differential scanning fluorimetry, T agg values were obtained by performing a nonlinear regression to a Boltzmann sigmoid function using GraphPad Prism.

    Techniques: Circular Dichroism, Thermal Shift Assay, Expressing, Centrifugation, Western Blot