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Software Package (V. 7.9.0.529), 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
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Custom Made Software, 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
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Software Package Matlab 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/software package matlab 7.9.0/product/MathWorks Inc
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software package matlab 7.9.0 - by Bioz Stars, 2026-03
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Matlab 7.9.0 Software, 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/matlab 7.9.0 software/product/MathWorks Inc
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matlab 7.9.0 software - by Bioz Stars, 2026-03
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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
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MathWorks Inc custom-made matlab software
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.
Custom Made Matlab Software, 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/custom-made matlab software/product/MathWorks Inc
Average 90 stars, based on 1 article reviews
custom-made matlab software - by Bioz Stars, 2026-03
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MathWorks Inc 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.
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/matlab version 7.9.0/product/MathWorks Inc
Average 90 stars, based on 1 article reviews
matlab version 7.9.0 - by Bioz Stars, 2026-03
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MathWorks Inc version 7.9.0.529 software
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.
Version 7.9.0.529 Software, 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/version 7.9.0.529 software/product/MathWorks Inc
Average 90 stars, based on 1 article reviews
version 7.9.0.529 software - by Bioz Stars, 2026-03
90/100 stars
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MathWorks Inc matlab software
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.
Matlab Software, 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/matlab software/product/MathWorks Inc
Average 90 stars, based on 1 article reviews
matlab software - by Bioz Stars, 2026-03
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MathWorks Inc matlab software 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.
Matlab Software Version 7 9 0, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/matlab software version 7 9 0/product/MathWorks Inc
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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.
Software Matlab 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/software matlab 7.9.0/product/MathWorks Inc
Average 90 stars, based on 1 article reviews
software matlab 7.9.0 - by Bioz Stars, 2026-03
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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