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SSDraw: software for generating comparative protein secondary structure diagrams

The program SSDraw generates publication-quality protein secondary structure diagrams from three-dimensional protein structures. To depict relationships between secondary structure and other protein features, diagrams can be colored by conservation score, B-factor, or custom scoring. Diagrams of hom...

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Detalles Bibliográficos
Autores principales: Chen, Ethan A., Porter, Lauren L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10541582/
https://www.ncbi.nlm.nih.gov/pubmed/37786684
http://dx.doi.org/10.1101/2023.08.25.554905
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author Chen, Ethan A.
Porter, Lauren L.
author_facet Chen, Ethan A.
Porter, Lauren L.
author_sort Chen, Ethan A.
collection PubMed
description The program SSDraw generates publication-quality protein secondary structure diagrams from three-dimensional protein structures. To depict relationships between secondary structure and other protein features, diagrams can be colored by conservation score, B-factor, or custom scoring. Diagrams of homologous proteins can be registered according to an input multiple sequence alignment. Linear visualization allows the user to stack registered diagrams, facilitating comparison of secondary structure and other properties among homologous proteins. SSDraw can be used to compare secondary structures of homologous proteins with both conserved and divergent folds. It can also generate one secondary structure diagram from an input protein structure of interest. The source code can be downloaded (https://github.com/ethanchen1301/SSDraw) and run locally for rapid structure generation, while a Google Colab notebook allows easy use.
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spelling pubmed-105415822023-11-14 SSDraw: software for generating comparative protein secondary structure diagrams Chen, Ethan A. Porter, Lauren L. bioRxiv Article The program SSDraw generates publication-quality protein secondary structure diagrams from three-dimensional protein structures. To depict relationships between secondary structure and other protein features, diagrams can be colored by conservation score, B-factor, or custom scoring. Diagrams of homologous proteins can be registered according to an input multiple sequence alignment. Linear visualization allows the user to stack registered diagrams, facilitating comparison of secondary structure and other properties among homologous proteins. SSDraw can be used to compare secondary structures of homologous proteins with both conserved and divergent folds. It can also generate one secondary structure diagram from an input protein structure of interest. The source code can be downloaded (https://github.com/ethanchen1301/SSDraw) and run locally for rapid structure generation, while a Google Colab notebook allows easy use. Cold Spring Harbor Laboratory 2023-11-10 /pmc/articles/PMC10541582/ /pubmed/37786684 http://dx.doi.org/10.1101/2023.08.25.554905 Text en https://creativecommons.org/publicdomain/zero/1.0/This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under a CC0 license (https://creativecommons.org/publicdomain/zero/1.0/) .
spellingShingle Article
Chen, Ethan A.
Porter, Lauren L.
SSDraw: software for generating comparative protein secondary structure diagrams
title SSDraw: software for generating comparative protein secondary structure diagrams
title_full SSDraw: software for generating comparative protein secondary structure diagrams
title_fullStr SSDraw: software for generating comparative protein secondary structure diagrams
title_full_unstemmed SSDraw: software for generating comparative protein secondary structure diagrams
title_short SSDraw: software for generating comparative protein secondary structure diagrams
title_sort ssdraw: software for generating comparative protein secondary structure diagrams
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10541582/
https://www.ncbi.nlm.nih.gov/pubmed/37786684
http://dx.doi.org/10.1101/2023.08.25.554905
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