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SS-map: Visualizing cooperative secondary structure elements in protein ensembles

We present SS-map, a tool to visualize the secondary structure content of ensembles of proteins. When generating ensembles of intrinsically disordered proteins, we lose the understanding a single native structure gives for folded proteins. It then becomes difficult to visualize the composition of th...

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Detalles Bibliográficos
Autores principales: Iglesias, Jelisa, Sanchez-Martínez, Melchor, Crehuet, Ramon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5424797/
https://www.ncbi.nlm.nih.gov/pubmed/28516013
http://dx.doi.org/10.4161/idp.25323
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author Iglesias, Jelisa
Sanchez-Martínez, Melchor
Crehuet, Ramon
author_facet Iglesias, Jelisa
Sanchez-Martínez, Melchor
Crehuet, Ramon
author_sort Iglesias, Jelisa
collection PubMed
description We present SS-map, a tool to visualize the secondary structure content of ensembles of proteins. When generating ensembles of intrinsically disordered proteins, we lose the understanding a single native structure gives for folded proteins. It then becomes difficult to visualize the composition of the ensembles or to detect transient helices such as MoRFs. Conformational propensities for single residues also hide the nature of cooperative structures. Here we show how SS-map describes folded and unfolded ensembles of some peptides and gives a new view of the ensembles used to describe intrinsically disordered proteins with residual structure in computational and NMR experiments. This tool is implemented in an open-source python code located at code.google.com/p/ss-map
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spelling pubmed-54247972017-05-17 SS-map: Visualizing cooperative secondary structure elements in protein ensembles Iglesias, Jelisa Sanchez-Martínez, Melchor Crehuet, Ramon Intrinsically Disord Proteins Short Communication We present SS-map, a tool to visualize the secondary structure content of ensembles of proteins. When generating ensembles of intrinsically disordered proteins, we lose the understanding a single native structure gives for folded proteins. It then becomes difficult to visualize the composition of the ensembles or to detect transient helices such as MoRFs. Conformational propensities for single residues also hide the nature of cooperative structures. Here we show how SS-map describes folded and unfolded ensembles of some peptides and gives a new view of the ensembles used to describe intrinsically disordered proteins with residual structure in computational and NMR experiments. This tool is implemented in an open-source python code located at code.google.com/p/ss-map Taylor & Francis 2013-06-10 /pmc/articles/PMC5424797/ /pubmed/28516013 http://dx.doi.org/10.4161/idp.25323 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Short Communication
Iglesias, Jelisa
Sanchez-Martínez, Melchor
Crehuet, Ramon
SS-map: Visualizing cooperative secondary structure elements in protein ensembles
title SS-map: Visualizing cooperative secondary structure elements in protein ensembles
title_full SS-map: Visualizing cooperative secondary structure elements in protein ensembles
title_fullStr SS-map: Visualizing cooperative secondary structure elements in protein ensembles
title_full_unstemmed SS-map: Visualizing cooperative secondary structure elements in protein ensembles
title_short SS-map: Visualizing cooperative secondary structure elements in protein ensembles
title_sort ss-map: visualizing cooperative secondary structure elements in protein ensembles
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5424797/
https://www.ncbi.nlm.nih.gov/pubmed/28516013
http://dx.doi.org/10.4161/idp.25323
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