Dixon plot was created in Origin software (OriginLab, Northampton, MA, USA). Ki for uncompetitive inhibition was calculated from Dixon plot as follows: Slope = 1/Vmax × Ki. Vmax for AChE was obtained experimentally (as described in previous section) and calculated in Origin software (OriginLab, Northampton, MA, USA) using nonlinear Hill fitting with coefficient of cooperativity n = 1.
Origin software
Manufactured by OriginLab
Sourced in United States, United Kingdom
Origin is a data analysis and graphing software. It provides tools for data processing, visualization, and analysis. The software allows users to import, manipulate, and visualize data in various formats.
Automatically generated - may contain errors
Lab products found in correlation
Spss software, by IBM (35 mentions)
Microcal itc200, by GE Healthcare (10 mentions)
Microcal itc200, by Malvern Panalytical (9 mentions)
Spss statistics software, by IBM (6 mentions)
Matlab, by MathWorks (5 mentions)
Itc200, by Malvern Panalytical (5 mentions)
Axopatch 200b, by Molecular Devices (4 mentions)
Microcal auto itc200, by GE Healthcare (4 mentions)
Prism 8, by GraphPad (4 mentions)
Sas version 9, by SAS Institute (4 mentions)
Clampfit 10, by Molecular Devices (4 mentions)
Atpγs, by Roche (3 mentions)
Microcal auto itc200, by Malvern Panalytical (3 mentions)
Itc200, by GE Healthcare (3 mentions)
Spss statistic, by IBM (3 mentions)
Prism software, by GraphPad (3 mentions)
Vp itc microcalorimeter, by GE Healthcare (3 mentions)
Nicolet 6700, by Thermo Fisher Scientific (3 mentions)
Opus software, by Bruker (2 mentions)
Vp itc system, by GE Healthcare (2 mentions)
583 protocols using origin software
1
Dixon Plot Analysis for AChE Inhibition
2
Fluorescence-Based Kinetic Assays for Cdc48
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Unfolding assays were measured by monitoring the loss of fluorescence for K48-GREEN (excitation 500 nm, emission 520 nm) and K48-RED (excitation 565 nm, emission 585 nm) using QuantaMaster spectrofluorometer (PTI) at 30 °C.
For single turnover assays, substrate K48-GREEN or K48-RED at a final concentration of 0.2 μM was first preincubated with 100 μM creatine phosphate, Ufd1/Npl4 heterodimer (17 μM final), and 4X ATP Regeneration Mix. The sample was then diluted by adding an equal volume of Cdc48 (17 μM final), BSA (0.5 mg/ml final), 100 μM creatine phosphate and 1X ATP Regeneration Mix. Single-turnover curves were fit to single exponential (K48-GREEN) and double-exponential decay (K48-RED) using Origin Software (Originlab, Northampton, MA).
For multiple-turnover assays, K48-RED substrate at 20 μM was first preincubated with Ufd1/Npl4 heterodimer (15 μM final) and creatine phosphate (100 μM final), before adding an equal volume of Cdc48 (0.2 μM final) with BSA (0.5 mg/ml final) and 1X ATP Regeneration Mix (final concentration). For Michaelis–Menten analyses, substrate concentrations were varied from 0.4 μM to 26 μM, with each condition repeated in triplicate. Calculated initial rates were fit directly to the Michaelis–Menten equation with nonlinear regression using Origin Software (Originlab, Northampton, MA).
For single turnover assays, substrate K48-GREEN or K48-RED at a final concentration of 0.2 μM was first preincubated with 100 μM creatine phosphate, Ufd1/Npl4 heterodimer (17 μM final), and 4X ATP Regeneration Mix. The sample was then diluted by adding an equal volume of Cdc48 (17 μM final), BSA (0.5 mg/ml final), 100 μM creatine phosphate and 1X ATP Regeneration Mix. Single-turnover curves were fit to single exponential (K48-GREEN) and double-exponential decay (K48-RED) using Origin Software (Originlab, Northampton, MA).
For multiple-turnover assays, K48-RED substrate at 20 μM was first preincubated with Ufd1/Npl4 heterodimer (15 μM final) and creatine phosphate (100 μM final), before adding an equal volume of Cdc48 (0.2 μM final) with BSA (0.5 mg/ml final) and 1X ATP Regeneration Mix (final concentration). For Michaelis–Menten analyses, substrate concentrations were varied from 0.4 μM to 26 μM, with each condition repeated in triplicate. Calculated initial rates were fit directly to the Michaelis–Menten equation with nonlinear regression using Origin Software (Originlab, Northampton, MA).
3
Raman Spectroscopy for Bacterial Identification
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By calculating the average intensities under each Raman shift for all the SERS spectra that were generated from E. coli (N = 800) and Shigella spp (N = 800), respectively, average Raman spectra were then obtained. 20% of standard deviation (SD) was also calculated and visualized as shaded region around the average SERS spectra for E. coli and Shigella spp. Average Raman spectra with standard error bands were plotted using Origin software (OriginLab, United States). The width of the error bands showed the reproducibility of Raman spectra. The wider the error band, the worse the reproducibility.
4
Isothermal Titration Calorimetry of Kinase Interactions
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All ITC experiments were performed on itc200 instrument (GE Healthcare). Prior to ITC titration, proteins and peptides were buffer exchanged into 10 mM HEPES pH 7.4, 500 mM NaCl, 0.05% P20 surfactant. ITC experiments with Aurora Awt kinase were performed in buffer containing 50 mM HEPES pH 7.4, 100 mM Mg(CH3COO)2, 100 mM NaCl, 1 mM ATP, 1 mM DTT, 0.01% v/v P20. Titrations experiments were conducted at 25°C with an initial 0.4 μl injection at a duration of 0.8 s, followed by 19 or 29 injections of 2 μl at a duration of 4 s with 120, 180 or 200 s spacing for Aurora AD274N, Aurora AWT and CK2α kinase binding assays, respectively. In the Aurora AD274N and Aurora AWT binding assays, 50 μM solution of the titrant was injected into 5 μM kinase solution in the cell. For the determination of binding affinity between CK2α and its interacting partners, 100 μM of CK2β peptide or RAD-CK2β display were titrated into 10 μM CK2α kinase solution. Binding isotherms were fit by non-linear regression using the single-site model provided by ORIGIN software (Origin Lab). The stoichiometry of the interaction (N), equilibrium association constant (KA) and change of enthalpy (ΔH) were floated during the fitting.
5
Evaluating Essential Oil Insecticidal Activity
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The LC50 or IC50 values were calculated by POLO-Plus software (Robertson et al., 2017) . Data was only used when the probit model was accepted (chi-square goodness-of-fit test) and all the bioassay data were well described by the probit model (χ 2 test, p > 0.05). Pearson correlation analysis (P < 0.05) was used to determine the cross-resistance between EOs and insecticides (PROC CORR). The IC50 values were calculated by plotting the percentage enzyme inhibition versus concentration of EOs. Analysis of variance (ANOVA) followed by LSD mean separation was used to test the differences in the levels of IC50 values using SAS v. 9.4 software (Institute, 2017) . The comparison charts were prepared using Origin software (OriginLab, 2018).
6
Statistical Analysis of Experimental Data
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The results of the experiments were statistically analyzed using the Origin software (version 2020, OriginLab, United States). All the data were presented as the mean ± SD. Statistical analyses among the multiple group data were carried out using a one-way analysis of variance (ANOVA) test to determine the significant differences. Tukey’s post-hoc test was used to determine the difference between any two groups with *p < 0.05 considered statistically significant.
7
SSRP1 Histone Binding Kinetics
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SSRP1 binding to histone H2A–H2B or H3–H4 was determined at 25 °C by using a MicroCal iTC200 microcalorimeter (Malvern Instruments Ltd., UK). All proteins were buffer-exchanged into 20 mm HEPES, pH 7.5, 200 mm NaCl, 1 mm DTT. Histone H2A–H2B or H3–H4 was loaded into the cell at a concentration of 20–30 μm , and SSRP1 variants were loaded into the syringe at a concentration 10 times higher than that in the cell. 20 injections (2 μl each) were added every 180 s to the cell. For control experiments, buffer or SSRP1 was injected into the cell containing histone or buffer, respectively. ITC data were generated by subtracting the raw data from the control experiment and were analyzed using Origin software (version 7, OriginLab).
8
Standardized Analytical Curve Fitting
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To build the plots of color intensity (in relative units, RU) or OD (y) versus the analyte concentrations (x) and fit them using a four-parameter logistic function, Origin software from OriginLab (Northampton, MA, USA) was applied. The LODs, working ranges, and cutoffs were determined in accordance with Uhrovcik (2014) [27 (link)].
9
Thermal Stability Analysis of rPspA Fusion Proteins
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Secondary structures and stability of purified rPspA-FL-PdT and rPspA-RL-PdT at different temperatures were verified by circular dichroism (CD) spectroscopy, using a JASCO J-810 spectropolarimeter (Japan Spectroscopic, Tokyo, Japan). rPspA-FL-PdT and rPspA-RL-PdT samples were prepared in 20 mM phosphate buffer pH 7.0. Measurements were taken from 185 to 260 nm and final CD spectra were obtained from the mean of five measurements. The fusion proteins were heated (1°C/min) from 2°C to 98°C and cooled back to 2°C (1°C/min), and their melting temperature (Tm) was calculated using Origin software (OriginLab Corporation) by fitting the sigmoid curves using Boltzmann function and finding the minimum value of its derivative at X-axis, which represents the sigmoid inflection point. Deconvolution was calculated based on the Dichroweb (Whitmore and Wallace, 2004 (link)) online database and the CDSSTR (Sreerama and Woody, 2000 (link)) algorithm.
10
Statistical analysis of results
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Statistical analysis of the results was carried out using the Origin software (OriginLab Corporation, USA) and the R software (R Foundation for Statistical Computing, Vienna, Austria). The Kruskal–Wallis test and Mann–Whitney test were used to compare the independent samples. The differences were considered statistically significant when the p-value was less than 0.05.
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