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multimodal gaussian curves  (OriginLab corp)


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    Structured Review

    OriginLab corp multimodal gaussian curves
    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 <t>Gaussian</t> curves to determine the position of each peak that corresponds to the most probable rupture force.
    Multimodal Gaussian Curves, 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/result/multimodal gaussian curves/product/OriginLab corp
    Average 90 stars, based on 1 article reviews
    multimodal gaussian curves - by Bioz Stars, 2026-06
    90/100 stars

    Images

    1) Product Images from "Direct evidence for specific interactions of the fibrinogen ?C-domains with the central E region and with each other"

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

    Journal:

    doi: 10.1021/bi700944j

    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.
    Figure Legend 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.

    Techniques Used: Derivative Assay

    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.
    Figure Legend 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.

    Techniques Used:

    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.
    Figure Legend 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.

    Techniques Used: Negative Control



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    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 <t>Gaussian</t> curves to determine the position of each peak that corresponds to the most probable rupture force.
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    Image Search Results


    Journal: bioRxiv

    Article Title: Landing on a dime: the biomechanics and kinematics of lovebirds ( Agapornis roseicollis ) landing on a swinging perch

    doi: 10.1101/2024.07.21.604435

    Figure Lengend Snippet:

    Article Snippet: A multimodal Gaussian curve fitting algorithm (Mathworks, USA) was used to determine the frequency distribution (number of landings) of the birds’ landing phases relative to the perch’s motion ( ).

    Techniques:

    Gaussian fit (A) SD: R 2 = 0.9199 and (B) OD: R 2 = 0.8933. (See ). The bimodal ratio of the left (0) versus right (+π) landing peaks for SD landings is 0.160, and for left (2π) versus right (+π) OD landing peaks is 0.640. The 3rd minor landing mode centered at ∼ ¹¹⁄₁₂ π for SD landings is 0.0457 and none for OD landings.

    Journal: bioRxiv

    Article Title: Landing on a dime: the biomechanics and kinematics of lovebirds ( Agapornis roseicollis ) landing on a swinging perch

    doi: 10.1101/2024.07.21.604435

    Figure Lengend Snippet: Gaussian fit (A) SD: R 2 = 0.9199 and (B) OD: R 2 = 0.8933. (See ). The bimodal ratio of the left (0) versus right (+π) landing peaks for SD landings is 0.160, and for left (2π) versus right (+π) OD landing peaks is 0.640. The 3rd minor landing mode centered at ∼ ¹¹⁄₁₂ π for SD landings is 0.0457 and none for OD landings.

    Article Snippet: A multimodal Gaussian curve fitting algorithm (Mathworks, USA) was used to determine the frequency distribution (number of landings) of the birds’ landing phases relative to the perch’s motion ( ).

    Techniques:

    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.

    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

    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.

    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:

    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.

    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