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Originpro 8.5g

Manufactured by OriginLab
Sourced in United States

OriginPro 8.5G is an advanced data analysis and graphing software. It provides tools for data manipulation, visualization, and statistical analysis. The software supports a variety of data formats and offers features for curve fitting, peak analysis, and image processing.

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8 protocols using originpro 8.5g

1

Biosensor Characterization of Amyloid-β Binding

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BLI experiments were performed using an Octet RED96 instrument (fortéBIO, PALL Life Science, Menlo Park, USA). N-terminally biotinylated Aβ(1–42) was dissolved in HFIP, lyophilized and dissolved in 2 mM aqueous sodium hydroxide (1 mg/ml) in order to destroy any pre-existing aggregates. The Aβ(1–42) solution was neutralized by dilution in running buffer (20 mM sodium phosphate buffer, pH 7.4) to a final concentration of 20 μg/ml and directly immobilized on Super Streptavidin biosensors (SSA) (fortéBIO, PALL Life Science, Menlo Park, USA) to a final depth of 3 nm. Ligand biosensors and reference biosensors were quenched with 20 μg/ml biotin for 7 min.
For KD determinations, the binding of a dilution series of DB3 (200, 100, 50, 25, 12.5, 6.25, 3.125 μM) or DBDB3 (20, 10, 5, 2.5, 1.25, 0.625, 0.3125 μM) was detected in parallel to the ligand biosensors and reference biosensors. A separate buffer cycle was used for double referencing. For evaluation, steady state response levels were plotted against the applied peptide concentrations and fitted according to Langmuir´s 1:1 binding model (Hill function with n = 1, OriginPro 8.5G, OriginLab, Northampton, USA).
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2

Plant Growth and Physiology Analysis

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The software programs R 3.4.2 [121 ] and Origin Pro 8.5G (OriginLab, Northampton, MA, USA) were used for statistical analyses and figure generation. Data of plant height, stem diameter, biomass of each tissue, gas exchange, anatomical traits and hormone concentrations were analyzed. One-way ANOVA was applied to compare the means between different treatments. Normality and homogeneity of variances were assessed visually by plotting residuals. Logarithmic (log2) transformation was applied to achieve normal distribution if necessary. When p-value < 0.05, Tukey test was applied as post-hoc for pairwise analysis.
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3

Tensile Testing of Material Samples

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Tensile testing was conducted on a ZWICK & ROELL Z2.5 instrument (Zwick ROELL, Ulm, Germany) equipped with an air conditioner at 24.9 ± 0.3 °C. All measurements were performed with a strain rate of 0.25 mm·s−1 and a loading speed of 25 mm·min−1. The cross section of the specimen was taken at three different places and averaged. The contact pressure was 0.8 bar. Tensile data (Young’s modulus E, toughness UT, and yield strength σy) reported herein were averages taken from at least three specimens per sample. The Young’s modulus (E) was calculated in the linear region of 0.05% to 0.20% elongation. Errors were given as maximum error. The data were collected and analyzed with the computer program testXpert II (Zwick ROELL) or ORIGINPRO 8.5G (Originlab, Northampton, MA, USA).
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4

Quantifying Microtubule Width via STED

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Chol-PEG-KK114 stained STED images of ATs and TTs were aligned. ROIs of 50 pixels × 30 pixels (pixel size 16.23 nm × 16.23 nm) were manually selected and used for fluorescence intensity plot profiling. AT and TT signal profiles were fitted by a 2-peak Gaussian function using OriginPro 8.5G to calculate FWHM as a measure of tubule width.
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5

Quantifying Aβ Fibrilization Inhibition

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The Thioflavin T (ThT) assay is a commonly used assay to visualize and quantify the fibrilisation of Aβ, since this dye binds to amyloidogenic cross-β-sheet structures. While Aβ aggregates into fibrils, the ThT fluorescence intensities increase until a saturation level is accomplished. Within this test, we analysed the inhibitory function of RD2 on the Aβ(1-42) fibril formation. 20 µM Aβ(1-42) was incubated with 5 µM ThT and different concentrations of RD2 (serial dilution from 80 µM till 1.25 µM) for IC50 calculation. ThT fluorescence was monitored over 21 h every 5 min at λex = 440 nm and λem = 490 nm in a fluorescence plate reader (Polarstar Optima, Germany) at 37 °C. Correction was done using all supplements without Aβ. For data evaluation, the fibril masses were determined by subtracting the baseline fluorescence intensities from the top and normalised to the Aβ control to calculate the inhibition in percent. The IC50 resulted from the compound concentration at the inflection point obtained by a logistic fit of the data (OriginPro 8.5 G, OriginLab, USA).
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6

SPR Analysis of DISC1 Binding

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SPR measurements were performed using a Biacore T200 instrument (GE Healthcare, Sweden) at 25°C with PBS/0.05% Tween-20, pH 7.4 as running buffer. For preparation of the flow cells, a CM5 sensor chip (GE Healthcare, Sweden) was activated with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) / N-hydroxysuccinimide (NHS) (0.2 M / 0.05 M), the DISC1 fragment comprising residues 691–836 (DISC1691-836) (30 μg/mL) diluted in 10 mM sodium acetate, pH 4.0. It was immobilized to a final level of 250 RU, and the flow cell was deactivated with 1 M ethanolamine-HCl. A reference flow cell was activated and deactivated only. Afterwards, VHH B5 at concentrations ranging from 19 nM to 1.5 μM was injected in a single cycle without regeneration. The sensorgrams were double referenced using the reference flow cell and a buffer cycle, while evaluation was performed by plotting the respective response levels against the applied VHH B5 concentrations. The curves were fitted using Langmuir's 1:1 binding model (Hill function with n = 1, OriginPro 8.5G, OriginLab, Northampton, USA).
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7

FTIR Spectroscopy of Sample Analysis

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FTIR was conducted on an Alpha FTIR Spectrophotometer (Bruker Optik GmbH, Bremen, Germany) in the attenuated total reflection (ATR) mode. The measurements were performed at room temperature between wavenumbers of 4000 and 400 cm−1 with a resolution of 4 cm−1. The samples were measured with 64 scans. Baseline corrections of the spectra were automatically performed by the baseline correction tool integrated into the software. The peaks were normalized by dividing through the highest measured signal intensity. The peak maximum was determined manually using OriginPro 8.5 G (OriginLab, Northampton, MA, USA).
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8

Voltammogram Data Analysis Protocol

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Cyclic and linear scan voltammogram presentations follow the IUPAC voltammogram convention with positive potential and anodic current in the positive x-axis and positive y-axis, respectively. For analysis of the experimental raw data, the standard accessory PATCHMASTER software (versions 2x74 and 2x90.2) of the measuring system was used. Further processing of data, statistics, and graphical presentations were carried out using OriginPro 8.5G and CorelDRAW X4. Values are mean ± SEM (or ± SD if explicitly stated).
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