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origin software  (OriginLab corp)


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    OriginLab corp origin software
    Origin Software, supplied by OriginLab corp, 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/data+fitting+software+origin(pro)+version+2016/origin+software/pmc09412253-172-8-15
    Average 90 stars, based on 1 article reviews
    origin software - by Bioz Stars, 2026-11
    90/100 stars

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    Related Articles

    other:

    Article Title: c-di-AMP determines the hierarchical organization of bacterial RCK proteins
    Article Snippet: In the Pyranine-fluorescence-based K+ flux assay, we focused on the initial fast phase of the individual fluorescence quenching curves and estimated time constants by fitting the first 50 s after CCCP addition (50-100 s) with a one-phase exponential equation y = y0 + A × e−(x−x0)/τ using the Origin software (OriginLab), where A is amplitude, x0 is the initial fit point, y0 corresponds to the plateau and τ is the time constant.

    Article Title: Synergistic mastery: Advancing mechanical and electrical harmony in conducting polymer hydrogel bioelectronics
    Article Snippet: X-ray diffraction (XRD) patterns were collected on a D8 ADVANCE X-ray diffractometer (Bruker AXS GmbH, Karlsruhe, Germany) using Cu-Kα radiation operated at 40.0 kV and 120 mA.

    Article Title: Differences in macrophage pyroptosis and polarization induced by nano-/micro-calcium oxalate crystals.
    Article Snippet: Nano Measurer 1.2 software was used to measure the size of the photographed samples, and the statistics were normally fitted in Origin (Version 2021, OriginLab Corporation, Northampton, MA, USA) software.

    Article Title: Fragment-Based Development of Small Molecule Inhibitors Targeting Mycobacterium tuberculosis Cholesterol Metabolism.
    Article Snippet: Samples were either analyzed in quartz cuvettes with a 1 cm path length using a CARY400 UV−vis spectrophotometer (Varian, U.K.), or in UV-star 96-well microplates (Greiner Bio-one, U.K.) using a CLARIOstar microplate reader (BMG Labtech, Germany) in absorbance mode.

    Isolation:

    Article Title: Dysregulated neural coding in the vagus nerve during long sepsis
    Article Snippet: .. Isolated unit firing rates were exported to Origin software (OriginLab, Northampton, MA) for graph generation and statistical comparisons. .. Waveforms were examined with custom written MATLAB scripts.

    Software:

    Article Title: Dysregulated neural coding in the vagus nerve during long sepsis
    Article Snippet: .. Isolated unit firing rates were exported to Origin software (OriginLab, Northampton, MA) for graph generation and statistical comparisons. .. Waveforms were examined with custom written MATLAB scripts.

    Article Title: Fragment-Based Development of Small Molecule Inhibitors Targeting Mycobacterium tuberculosis Cholesterol Metabolism.
    Article Snippet: .. Data fitting and analysis were performed using Origin software (OriginLab, Northampton, MA) or GraphPad Prism 5.01 (GraphPad Software, San Diego, USA). ..

    Article Title: Wet-electrospun porous freeform scaffold enhances colonisation of cells
    Article Snippet: .. Statistical analyses and plotting were conducted using Origin software (OriginLab Corporation, USA). ..

    Article Title: Supporting Information for NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein
    Article Snippet: .. Origin software (OriginLab) was used to graph DFS plots and fit histograms of rupture force distributions, applying various force spectroscopy models, as described (11, 12). ..

    Force Spectroscopy:

    Article Title: Supporting Information for NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein
    Article Snippet: .. Origin software (OriginLab) was used to graph DFS plots and fit histograms of rupture force distributions, applying various force spectroscopy models, as described (11, 12). ..



    Similar Products

    data fitting software origin(pro) version 2016  (OriginLab corp)
    90
    OriginLab corp data fitting software origin(pro) version 2016
    a Simplified representation of the 70S ribosome with the AMK binding site indicated with the blue star. b The unbiased ( F o – F c ) difference electron density map of AMK bound near the decoding center is contoured at 2.3σ. c AMK binds within helix h44 of the decoding center where the AHB moiety forms three unique interactions. d Time courses of f[ 3 H]Met-Phe-Phe tripeptide formation with EF-Tu ternary complex (TC) (5 μM) and EF-G (5 µM) in the absence (black) and presence of 20 μM AMK (red). Solid lines represent the double exponential fit of the data with SEM from n = 3 independent experiments. e Time evolution of fluorescence traces obtained for the EF-G (5 μM) catalyzed movement of pyrene-labeled mRNA on 70S ribosomes (0.5 μM) in the presence of various concentrations (0-5 µM) of AMK. The inhibition of mRNA movement by AMK was estimated from amplitudes of the slow phase of fluorescence traces relative to the total transition (normalized to 1) indicative of inhibited fraction of the ribosomes. f The fraction of AMK-inhibited pre-TC plotted against AMK concentration. Data were fitted with hyperbolic function (solid line) and half-inhibitory concentration ( K I ) of AMK on the inhibition of translocation was estimated from mid-point of transition. Experiments were conducted in <t>triplicates</t> and error bars indicate the SEM of data.
    Data Fitting Software Origin(pro) Version 2016, supplied by OriginLab corp, 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/data+fitting+software+origin(pro)+version+2016/curve+fitting+software+origin+8+0/pmc10400623-114-4-12
    Average 90 stars, based on 1 article reviews
    data fitting software origin(pro) version 2016 - by Bioz Stars, 2026-11
    90/100 stars
    		  Buy from Supplier

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    a Simplified representation of the 70S ribosome with the AMK binding site indicated with the blue star. b The unbiased ( F o – F c ) difference electron density map of AMK bound near the decoding center is contoured at 2.3σ. c AMK binds within helix h44 of the decoding center where the AHB moiety forms three unique interactions. d Time courses of f[ 3 H]Met-Phe-Phe tripeptide formation with EF-Tu ternary complex (TC) (5 μM) and EF-G (5 µM) in the absence (black) and presence of 20 μM AMK (red). Solid lines represent the double exponential fit of the data with SEM from n = 3 independent experiments. e Time evolution of fluorescence traces obtained for the EF-G (5 μM) catalyzed movement of pyrene-labeled mRNA on 70S ribosomes (0.5 μM) in the presence of various concentrations (0-5 µM) of AMK. The inhibition of mRNA movement by AMK was estimated from amplitudes of the slow phase of fluorescence traces relative to the total transition (normalized to 1) indicative of inhibited fraction of the ribosomes. f The fraction of AMK-inhibited pre-TC plotted against AMK concentration. Data were fitted with hyperbolic function (solid line) and half-inhibitory concentration ( K I ) of AMK on the inhibition of translocation was estimated from mid-point of transition. Experiments were conducted in triplicates and error bars indicate the SEM of data.

    Journal: Nature Communications

    Article Title: Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome

    doi: 10.1038/s41467-023-40416-5

    Figure Lengend Snippet: a Simplified representation of the 70S ribosome with the AMK binding site indicated with the blue star. b The unbiased ( F o – F c ) difference electron density map of AMK bound near the decoding center is contoured at 2.3σ. c AMK binds within helix h44 of the decoding center where the AHB moiety forms three unique interactions. d Time courses of f[ 3 H]Met-Phe-Phe tripeptide formation with EF-Tu ternary complex (TC) (5 μM) and EF-G (5 µM) in the absence (black) and presence of 20 μM AMK (red). Solid lines represent the double exponential fit of the data with SEM from n = 3 independent experiments. e Time evolution of fluorescence traces obtained for the EF-G (5 μM) catalyzed movement of pyrene-labeled mRNA on 70S ribosomes (0.5 μM) in the presence of various concentrations (0-5 µM) of AMK. The inhibition of mRNA movement by AMK was estimated from amplitudes of the slow phase of fluorescence traces relative to the total transition (normalized to 1) indicative of inhibited fraction of the ribosomes. f The fraction of AMK-inhibited pre-TC plotted against AMK concentration. Data were fitted with hyperbolic function (solid line) and half-inhibitory concentration ( K I ) of AMK on the inhibition of translocation was estimated from mid-point of transition. Experiments were conducted in triplicates and error bars indicate the SEM of data.

    Article Snippet: Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Techniques: Binding Assay, Fluorescence, Labeling, Inhibition, Concentration Assay, Translocation Assay

    a Time courses of BOP-Met-Phe-Leu release from the P site of the ribosomes in pre-TC (0.1 μM) upon mixing with RF2 (1 μM) in the presence of various concentrations of AMK (0-1 μM). The near monophasic curves are fitted with double exponential function (solid lines) and the rates and amplitudes of the predominant fast phase (> 99%) were determined. The fraction inhibited was estimated from the fractional loss in fluorescence amplitude for a given AMK concentration considering the total amplitude of fluorescence transition (without AMK) as 1. b Fraction inhibition of RF2-mediated peptide release as the function of increasing concentrations of AMK. Solid line is the hyperbolic fit of data from which half-maximal inhibitory concentration ( K I ) of AMK for peptide release was estimated. c Time tra c es for Rayleigh light scattering upon splitting of post-TC ribosomes (0.5 μM) into subunits by the concerted action of RRF (20 μM) and EF-G (10 μM) in the presence of various concentrations of AMK (0–20 μM). The scattering traces were fitted with double exponential function and the rates and amplitudes of both the fast and slow phases were determined. d Fraction inhibition of RRF and EF-G-mediated ribosome splitting was estimated from the fractional loss of the amplitude of the fast phase considering amplitude of the entire transition without AMK as 1. The solid line represents the hyperbolic fit of the fraction inhibition plotted against AMK concentration from which the half-maximal concentration ( K I ) of AMK to inhibit ribosome recycling was estimated. Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Journal: Nature Communications

    Article Title: Molecular basis of the pleiotropic effects by the antibiotic amikacin on the ribosome

    doi: 10.1038/s41467-023-40416-5

    Figure Lengend Snippet: a Time courses of BOP-Met-Phe-Leu release from the P site of the ribosomes in pre-TC (0.1 μM) upon mixing with RF2 (1 μM) in the presence of various concentrations of AMK (0-1 μM). The near monophasic curves are fitted with double exponential function (solid lines) and the rates and amplitudes of the predominant fast phase (> 99%) were determined. The fraction inhibited was estimated from the fractional loss in fluorescence amplitude for a given AMK concentration considering the total amplitude of fluorescence transition (without AMK) as 1. b Fraction inhibition of RF2-mediated peptide release as the function of increasing concentrations of AMK. Solid line is the hyperbolic fit of data from which half-maximal inhibitory concentration ( K I ) of AMK for peptide release was estimated. c Time tra c es for Rayleigh light scattering upon splitting of post-TC ribosomes (0.5 μM) into subunits by the concerted action of RRF (20 μM) and EF-G (10 μM) in the presence of various concentrations of AMK (0–20 μM). The scattering traces were fitted with double exponential function and the rates and amplitudes of both the fast and slow phases were determined. d Fraction inhibition of RRF and EF-G-mediated ribosome splitting was estimated from the fractional loss of the amplitude of the fast phase considering amplitude of the entire transition without AMK as 1. The solid line represents the hyperbolic fit of the fraction inhibition plotted against AMK concentration from which the half-maximal concentration ( K I ) of AMK to inhibit ribosome recycling was estimated. Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Article Snippet: Experiments were conducted in triplicates, data were fitted in Origin(Pro), Version 2016 (OriginLab Corp.), and error bars indicate the SEM of data.

    Techniques: Fluorescence, Concentration Assay, Inhibition