PTMselect: optimization of protein modifications discovery by mass spectrometry

Discovery of protein modification sites relies on protein digestion by proteases and mass spectrometry (MS) identification of the modified peptides. Depending on proteases used and target protein sequence, this method yields highly variable coverage of modification sites. We introduce PTMselect, a d...

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Detalles Bibliográficos
Autores principales: Perchey, Renaud T., Tonini, Laure, Tosolini, Marie, Fournié, Jean-Jacques, Lopez, Frédéric, Besson, Arnaud, Pont, Frédéric
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414543/
https://www.ncbi.nlm.nih.gov/pubmed/30862887
http://dx.doi.org/10.1038/s41598-019-40873-3
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author Perchey, Renaud T.
Tonini, Laure
Tosolini, Marie
Fournié, Jean-Jacques
Lopez, Frédéric
Besson, Arnaud
Pont, Frédéric
author_facet Perchey, Renaud T.
Tonini, Laure
Tosolini, Marie
Fournié, Jean-Jacques
Lopez, Frédéric
Besson, Arnaud
Pont, Frédéric
author_sort Perchey, Renaud T.
collection PubMed
description Discovery of protein modification sites relies on protein digestion by proteases and mass spectrometry (MS) identification of the modified peptides. Depending on proteases used and target protein sequence, this method yields highly variable coverage of modification sites. We introduce PTMselect, a digestion-simulating software which tailors the optimal set of proteases for discovery of global or targeted modification from any single or multiple proteins.
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spelling pubmed-64145432019-03-14 PTMselect: optimization of protein modifications discovery by mass spectrometry Perchey, Renaud T. Tonini, Laure Tosolini, Marie Fournié, Jean-Jacques Lopez, Frédéric Besson, Arnaud Pont, Frédéric Sci Rep Article Discovery of protein modification sites relies on protein digestion by proteases and mass spectrometry (MS) identification of the modified peptides. Depending on proteases used and target protein sequence, this method yields highly variable coverage of modification sites. We introduce PTMselect, a digestion-simulating software which tailors the optimal set of proteases for discovery of global or targeted modification from any single or multiple proteins. Nature Publishing Group UK 2019-03-12 /pmc/articles/PMC6414543/ /pubmed/30862887 http://dx.doi.org/10.1038/s41598-019-40873-3 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Perchey, Renaud T.
Tonini, Laure
Tosolini, Marie
Fournié, Jean-Jacques
Lopez, Frédéric
Besson, Arnaud
Pont, Frédéric
PTMselect: optimization of protein modifications discovery by mass spectrometry
title PTMselect: optimization of protein modifications discovery by mass spectrometry
title_full PTMselect: optimization of protein modifications discovery by mass spectrometry
title_fullStr PTMselect: optimization of protein modifications discovery by mass spectrometry
title_full_unstemmed PTMselect: optimization of protein modifications discovery by mass spectrometry
title_short PTMselect: optimization of protein modifications discovery by mass spectrometry
title_sort ptmselect: optimization of protein modifications discovery by mass spectrometry
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414543/
https://www.ncbi.nlm.nih.gov/pubmed/30862887
http://dx.doi.org/10.1038/s41598-019-40873-3
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