A Protease for Middle Down Proteomics

We developed a method for restricted enzymatic proteolysis using the outer membrane protease T (OmpT) to produce large peptides (> 6.3 kDa on average) for mass spectrometry-based proteomics. Using this approach to analyze prefractionated high-mass HeLa proteins we identified 3,697 unique peptides...

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Detalles Bibliográficos
Autores principales: Wu, Cong, Tran, John C., Zamdborg, Leonid, Durbin, Kenneth R., Li, Mingxi, Ahlf, Dorothy R., Early, Bryan P., Thomas, Paul M., Sweedler, Jonathan V., Kelleher, Neil L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2012
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3430368/
https://www.ncbi.nlm.nih.gov/pubmed/22706673
http://dx.doi.org/10.1038/nmeth.2074
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author Wu, Cong
Tran, John C.
Zamdborg, Leonid
Durbin, Kenneth R.
Li, Mingxi
Ahlf, Dorothy R.
Early, Bryan P.
Thomas, Paul M.
Sweedler, Jonathan V.
Kelleher, Neil L.
author_facet Wu, Cong
Tran, John C.
Zamdborg, Leonid
Durbin, Kenneth R.
Li, Mingxi
Ahlf, Dorothy R.
Early, Bryan P.
Thomas, Paul M.
Sweedler, Jonathan V.
Kelleher, Neil L.
author_sort Wu, Cong
collection PubMed
description We developed a method for restricted enzymatic proteolysis using the outer membrane protease T (OmpT) to produce large peptides (> 6.3 kDa on average) for mass spectrometry-based proteomics. Using this approach to analyze prefractionated high-mass HeLa proteins we identified 3,697 unique peptides from 1,038 proteins. We demonstrated the ability of large OmpT peptides to differentiate closely related protein isoforms and to enable the detection of many post-translational modifications.
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spelling pubmed-34303682013-02-01 A Protease for Middle Down Proteomics Wu, Cong Tran, John C. Zamdborg, Leonid Durbin, Kenneth R. Li, Mingxi Ahlf, Dorothy R. Early, Bryan P. Thomas, Paul M. Sweedler, Jonathan V. Kelleher, Neil L. Nat Methods Article We developed a method for restricted enzymatic proteolysis using the outer membrane protease T (OmpT) to produce large peptides (> 6.3 kDa on average) for mass spectrometry-based proteomics. Using this approach to analyze prefractionated high-mass HeLa proteins we identified 3,697 unique peptides from 1,038 proteins. We demonstrated the ability of large OmpT peptides to differentiate closely related protein isoforms and to enable the detection of many post-translational modifications. 2012-06-17 /pmc/articles/PMC3430368/ /pubmed/22706673 http://dx.doi.org/10.1038/nmeth.2074 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Wu, Cong
Tran, John C.
Zamdborg, Leonid
Durbin, Kenneth R.
Li, Mingxi
Ahlf, Dorothy R.
Early, Bryan P.
Thomas, Paul M.
Sweedler, Jonathan V.
Kelleher, Neil L.
A Protease for Middle Down Proteomics
title A Protease for Middle Down Proteomics
title_full A Protease for Middle Down Proteomics
title_fullStr A Protease for Middle Down Proteomics
title_full_unstemmed A Protease for Middle Down Proteomics
title_short A Protease for Middle Down Proteomics
title_sort protease for middle down proteomics
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3430368/
https://www.ncbi.nlm.nih.gov/pubmed/22706673
http://dx.doi.org/10.1038/nmeth.2074
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