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single-phase exponential equation fitting  (GraphPad Software Inc)


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    GraphPad Software Inc single-phase exponential equation fitting
    Single Phase Exponential Equation Fitting, 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/single+phase+exponential+equation/exponential+curve+fitting/pmc10084761-61-6-37
    Average 90 stars, based on 1 article reviews
    single-phase exponential equation fitting - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Modification:

    Article Title: Loss of Snf5 induces formation of an aberrant SWI/SNF complex
    Article Snippet: intensities were normalized for loading bias using Microsoft Excel. .. Normalized band intensities were plotted as a function of time and fitted into single phase exponential equation using GraphPad (PRISM Version 6.0b). .. Overlays for different time points were made using the ggplot2 package i

    Residue:

    Article Title: Loss of Snf5 induces formation of an aberrant SWI/SNF complex
    Article Snippet: intensities were normalized for loading bias using Microsoft Excel. .. Normalized band intensities were plotted as a function of time and fitted into single phase exponential equation using GraphPad (PRISM Version 6.0b). .. Overlays for different time points were made using the ggplot2 package i

    Thin Layer Chromatography:

    Article Title: Loss of Snf5 induces formation of an aberrant SWI/SNF complex
    Article Snippet: intensities were normalized for loading bias using Microsoft Excel. .. Normalized band intensities were plotted as a function of time and fitted into single phase exponential equation using GraphPad (PRISM Version 6.0b). .. Overlays for different time points were made using the ggplot2 package i



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    (A–B) Nucleosomes modified at residue 53 of histone H2B were used for monitoring movement of DNA on the octamer surface. DNA cleavage products were resolved on a denaturing 6% polyacrylamide gel and visualized by phosphorimaging. Numbers on the right side of the gel image refer to number of nucleotides (nt) moved from the starting cleavage position (0). Nucleosomes were remodeled with WT (A), and Δsnf5 SWI/SNF (B) for 0, 5, 10, 20, 30, 40, 50, 60, 70, 80 and 160 s using 4.4 μM ATP. (C) The amount of DNA cleaved at starting position (0) was plotted versus time for WT SWI/SNF and Δsnf5 SWI/SNF. Rate constants (k) obtained by fitting data to single <t>exponential</t> function were 0.044± 0.004 s−1 (WT) and 0.016 ± 0.005 s−1 (Δsnf5). Bars and reported values are the mean ± SE from two replicates. (D) ATPase assays were performed in the same conditions as (A and B) and the released radioactive phosphate (Pi) was separated from non-hydrolyzed ATP by thin layer chromatography (TLC). The percentage Pi released is plotted as a function of time. ATP hydrolysis rates obtained were 0.9 μM s−1 (WT) and 0.7 μM s−1 (Δsnf5).
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    (A–B) Nucleosomes modified at residue 53 of histone H2B were used for monitoring movement of DNA on the octamer surface. DNA cleavage products were resolved on a denaturing 6% polyacrylamide gel and visualized by phosphorimaging. Numbers on the right side of the gel image refer to number of nucleotides (nt) moved from the starting cleavage position (0). Nucleosomes were remodeled with WT (A), and Δsnf5 SWI/SNF (B) for 0, 5, 10, 20, 30, 40, 50, 60, 70, 80 and 160 s using 4.4 μM ATP. (C) The amount of DNA cleaved at starting position (0) was plotted versus time for WT SWI/SNF and Δsnf5 SWI/SNF. Rate constants (k) obtained by fitting data to single <t>exponential</t> function were 0.044± 0.004 s−1 (WT) and 0.016 ± 0.005 s−1 (Δsnf5). Bars and reported values are the mean ± SE from two replicates. (D) ATPase assays were performed in the same conditions as (A and B) and the released radioactive phosphate (Pi) was separated from non-hydrolyzed ATP by thin layer chromatography (TLC). The percentage Pi released is plotted as a function of time. ATP hydrolysis rates obtained were 0.9 μM s−1 (WT) and 0.7 μM s−1 (Δsnf5).
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    Image Search Results


    (A–B) Nucleosomes modified at residue 53 of histone H2B were used for monitoring movement of DNA on the octamer surface. DNA cleavage products were resolved on a denaturing 6% polyacrylamide gel and visualized by phosphorimaging. Numbers on the right side of the gel image refer to number of nucleotides (nt) moved from the starting cleavage position (0). Nucleosomes were remodeled with WT (A), and Δsnf5 SWI/SNF (B) for 0, 5, 10, 20, 30, 40, 50, 60, 70, 80 and 160 s using 4.4 μM ATP. (C) The amount of DNA cleaved at starting position (0) was plotted versus time for WT SWI/SNF and Δsnf5 SWI/SNF. Rate constants (k) obtained by fitting data to single exponential function were 0.044± 0.004 s−1 (WT) and 0.016 ± 0.005 s−1 (Δsnf5). Bars and reported values are the mean ± SE from two replicates. (D) ATPase assays were performed in the same conditions as (A and B) and the released radioactive phosphate (Pi) was separated from non-hydrolyzed ATP by thin layer chromatography (TLC). The percentage Pi released is plotted as a function of time. ATP hydrolysis rates obtained were 0.9 μM s−1 (WT) and 0.7 μM s−1 (Δsnf5).

    Journal: Cell reports

    Article Title: Loss of Snf5 induces formation of an aberrant SWI/SNF complex

    doi: 10.1016/j.celrep.2017.02.017

    Figure Lengend Snippet: (A–B) Nucleosomes modified at residue 53 of histone H2B were used for monitoring movement of DNA on the octamer surface. DNA cleavage products were resolved on a denaturing 6% polyacrylamide gel and visualized by phosphorimaging. Numbers on the right side of the gel image refer to number of nucleotides (nt) moved from the starting cleavage position (0). Nucleosomes were remodeled with WT (A), and Δsnf5 SWI/SNF (B) for 0, 5, 10, 20, 30, 40, 50, 60, 70, 80 and 160 s using 4.4 μM ATP. (C) The amount of DNA cleaved at starting position (0) was plotted versus time for WT SWI/SNF and Δsnf5 SWI/SNF. Rate constants (k) obtained by fitting data to single exponential function were 0.044± 0.004 s−1 (WT) and 0.016 ± 0.005 s−1 (Δsnf5). Bars and reported values are the mean ± SE from two replicates. (D) ATPase assays were performed in the same conditions as (A and B) and the released radioactive phosphate (Pi) was separated from non-hydrolyzed ATP by thin layer chromatography (TLC). The percentage Pi released is plotted as a function of time. ATP hydrolysis rates obtained were 0.9 μM s−1 (WT) and 0.7 μM s−1 (Δsnf5).

    Article Snippet: Normalized band intensities were plotted as a function of time and fitted into single phase exponential equation using GraphPad (PRISM Version 6.0b).

    Techniques: Modification, Residue, Thin Layer Chromatography