Journal:

Article Title: Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other

doi: 10.1021/bi700944j

Figure Lengend Snippet: A, B, and C – interactions of the BβN-domains with the αC region, αC-domain, and αC-connector, respectively; D, E, and F - interactions of the βN-domains with the αC region, αC-domain, and αC-connector, respectively; G - interactions of the αC region with the BβN-domains treated with thrombin and thus converted to the βN-domains right on the surface; H - interactions of the αC-domain with the BβN-domains in the presence of 200 µg/ml anti-Bβ1-21 mAb; I – paired bars representing cumulative probabilities of forces >10 pN derived from A and D, B and E, and C and F. The dashed lines show the fitting with Gaussian curves to determine the position of each peak that corresponds to the most probable rupture force.

Article Snippet: The rupture force histograms were fit empirically with multimodal Gaussian curves using Origin 7.5 ® (OriginLab Corp., Northampton, MA) to determine the position of a peak that corresponds to the most probable rupture force.

Techniques: Derivative Assay

Journal:

Article Title: Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other

doi: 10.1021/bi700944j

Figure Lengend Snippet: A, B, and C - interactions of the αC region with NDSK, desA-NDSK, and desAB-NDSK, respectively; D and E - interactions of the αC-domain with NDSK and desA-NDSK, respectively; F – the same as in E, but in the presence of 200 µg/ml anti-Bβ1-21 mAb. The dashed lines show the fitting with Gaussian curves to determine the position of each peak that corresponds to the most probable rupture force.

Article Snippet: The rupture force histograms were fit empirically with multimodal Gaussian curves using Origin 7.5 ® (OriginLab Corp., Northampton, MA) to determine the position of a peak that corresponds to the most probable rupture force.

Techniques:

Journal:

Article Title: Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other

doi: 10.1021/bi700944j

Figure Lengend Snippet: A - interactions of the pedestal-bound αC region with the αC region coupled to a bead; B - the pedestal-bound αC-domain with the αC-domain coupled to a bead; C, D, and E – the pedestal-bound αC region, αC-domain, and αC-connector with the αC-connector coupled to a bead, respectively; F - the pedestal-bound αC-domain with the BSA-coated bead (negative control). The dashed lines show the fitting with Gaussian curves to determine the position of each peak that corresponds to the most probable rupture force.

Article Snippet: The rupture force histograms were fit empirically with multimodal Gaussian curves using Origin 7.5 ® (OriginLab Corp., Northampton, MA) to determine the position of a peak that corresponds to the most probable rupture force.

Techniques: Negative Control

Journal: ACS nano

Article Title: Stability of Ti 3 C 2 T x MXene Films and Devices under Clinical Sterilization Processes

doi: 10.1021/acsnano.3c01525

Figure Lengend Snippet: (A, B) Left: XRD patterns including pristine control and Parylene-C or textile backgrounds. Right: FWHM of the (002) peak for (A) thin-film devices and (B) MXtrodes (n = 2 for each condition). (C) Raman spectra including pristine controls and Parylene-C background for thin-film devices. (n = 2 samples for each condition). (D) Normalized Gaussian-fitted A1g(C) peak for thin-film devices. (E) Right-shifting Normalized Gaussian-fitted A1g(C) peak for increasingly visually damaged thin-film samples after H2O2 gas plasma sterilization.

Article Snippet: After collection, peak amplitude and FWHM peak values were confirmed using OriginLab, which fitted the peak with a gaussian curve for calculation.

Techniques: Control, Clinical Proteomics

Journal: eLife

Article Title: Homo-oligomerization of the human adenosine A 2A receptor is driven by the intrinsically disordered C-terminus

doi: 10.7554/eLife.66662

Figure Lengend Snippet: The SEC data is recorded every second as absorbance at 280 nm. The baseline is corrected to ensure uniform fitting and integration across the peaks. The areas under the curve, resulting from a multiple-Gaussian curve fit, express the population of each oligomeric species. The reported standard errors of integration are within a 95% confidence interval and are calculated from the variance of the fit, not experimental errors. The levels of high-molecular-weight oligomer and dimer are expressed relative to the monomeric population in arbitrary units. A representative calculation defining the oligomer levels is given in the box.

Article Snippet: SEC chromatograms were analyzed using OriginLab using the nonlinear curve fit (Gaussian) function.

Techniques: High Molecular Weight

Journal: eLife

Article Title: Homo-oligomerization of the human adenosine A 2A receptor is driven by the intrinsically disordered C-terminus

doi: 10.7554/eLife.66662

Figure Lengend Snippet: ( A ) Curve fitting using OriginLab of all A 2A R variants used in the main text of this study, listed by the order they appear. By default, each oligomeric peak is fitted with one curve using Gaussian distribution and displayed by different color shades, with the high-molecular-weight (HMW) oligomer eluted first (dark orange), followed by the dimer (lighter orange), followed by the monomer (lightest orange). However, the HMW oligomer peak in some cases cannot be fitted with one curve and thus is fitted with two curves instead. This discrepancy can be explained by variation in HMW oligomerization order among the variants. The identity of each peak is confirmed with western blotting. The value and error from the curve fitting of each peak are given in . ( B ) Data distribution of all variants used in this study in comparison to five experimental replicates of A 2A R-WT. The C-terminally truncated mutants are represented by different shades of green in increasing darkness corresponding to the increased length of the C-terminus, with the lightest shade representing the mutant with the shortest C-terminus (A316ΔC) and the darkest shade for the mutant with the longest C-terminus (P395ΔC). The levels of dimer and HMW oligomer are expressed relative to the monomeric population in arbitrary unit, with reported errors calculated from the variance of the fit, not experimental variation. There are significant variations in the dimer and HMW oligomer levels among the WT replicates, stemming from experimental errors. These variations are mitigated when the two parameters are added as the data distribution becomes more uniform. Also, the oligomerization levels of the WT replicates are consistently higher than the mutated and truncated variants. Figure 1—figure supplement 2—source data 1. Raw size-exclusion chromatography data of five experimental replicates of A 2A R-WT.

Article Snippet: SEC chromatograms were analyzed using OriginLab using the nonlinear curve fit (Gaussian) function.

Techniques: High Molecular Weight, Western Blot, Comparison, Mutagenesis, Size-exclusion Chromatography