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data processing software matlab version 7.9.0  (MathWorks Inc)


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    Structured Review

    MathWorks Inc data processing software matlab version 7.9.0
    Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.
    Data Processing Software Matlab Version 7.9.0, supplied by MathWorks Inc, 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/data processing software matlab version 7.9.0/product/MathWorks Inc
    Average 90 stars, based on 1 article reviews
    data processing software matlab version 7.9.0 - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "Quantum dots and prion proteins"

    Article Title: Quantum dots and prion proteins

    Journal: Prion

    doi: 10.4161/pri.26524

    Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.
    Figure Legend Snippet: Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.

    Techniques Used: Software



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    data processing software matlab version 7.9.0  (MathWorks Inc)
    90
    MathWorks Inc data processing software matlab version 7.9.0
    Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.
    Data Processing Software Matlab Version 7.9.0, supplied by MathWorks Inc, 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/data processing software matlab version 7.9.0/product/MathWorks Inc
    Average 90 stars, based on 1 article reviews
    data processing software matlab version 7.9.0 - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.

    Journal: Prion

    Article Title: Quantum dots and prion proteins

    doi: 10.4161/pri.26524

    Figure Lengend Snippet: Figure 1. Three-dimensional (3D) structure of human PrP. The structure of the α-helical form of rPrP(90–231) resembles that of PrPC. rPrP(90–231) is viewed from the interface where PrPSc is thought to bind to PrPC. The color scheme is as follows: α-helices A (residues 144–157), B (172–193), and C (200–227) in pink; disulphide between Cys-179 and Cys-214 in yellow; conserved hydrophobic region composed of residues 113–126 in red; loops in gray; residues 129–134 in green encompassing strand S1 and residues 159–165 in blue encompassing strand S2; the arrows span residues 129–131 and 161–163, as these show a closer resemblance to β-sheet (155).1 The data source was the internet proteomic database Expasy (www.expasy.org). For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.

    Article Snippet: For data processing software Matlab version 7.9.0 (The MathWorks, Inc.) was used.

    Techniques: Software