Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.

The current advances in mass spectrometry technology have led to the possibility of analyzing more complex biological samples such as entire proteomes. Here, we describe a new and powerful methodology that combines the use of the metalloendopeptidase Lys-N and strong cation exchange with mass spectr...

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Main Authors: Taouatas, N, Mohammed, S, Heck, A
Format: Journal article
Language:English
Published: 2011
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author Taouatas, N
Mohammed, S
Heck, A
author_facet Taouatas, N
Mohammed, S
Heck, A
author_sort Taouatas, N
collection OXFORD
description The current advances in mass spectrometry technology have led to the possibility of analyzing more complex biological samples such as entire proteomes. Here, we describe a new and powerful methodology that combines the use of the metalloendopeptidase Lys-N and strong cation exchange with mass spectrometric analysis. The approach described here allows one to separate peptides with different functional groups. The peptides we are able to isolate are N-terminal peptides, phosphorylated peptides with a single lysine, peptides with a single basic residue (lysine), and peptides with multiply basic residues. When this separation strategy is combined with tandem mass spectrometry that involves both collision-induced dissociation and electron transfer dissociation, one can achieve an optimal targeted strategy for proteome analysis.
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spelling oxford-uuid:fe257933-3a75-4aff-b782-1b4bd28f5e282022-03-27T13:34:05ZExploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fe257933-3a75-4aff-b782-1b4bd28f5e28EnglishSymplectic Elements at Oxford2011Taouatas, NMohammed, SHeck, AThe current advances in mass spectrometry technology have led to the possibility of analyzing more complex biological samples such as entire proteomes. Here, we describe a new and powerful methodology that combines the use of the metalloendopeptidase Lys-N and strong cation exchange with mass spectrometric analysis. The approach described here allows one to separate peptides with different functional groups. The peptides we are able to isolate are N-terminal peptides, phosphorylated peptides with a single lysine, peptides with a single basic residue (lysine), and peptides with multiply basic residues. When this separation strategy is combined with tandem mass spectrometry that involves both collision-induced dissociation and electron transfer dissociation, one can achieve an optimal targeted strategy for proteome analysis.
spellingShingle Taouatas, N
Mohammed, S
Heck, A
Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.
title Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.
title_full Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.
title_fullStr Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.
title_full_unstemmed Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.
title_short Exploring new proteome space: combining Lys-N proteolytic digestion and strong cation exchange (SCX) separation in peptide-centric MS-driven proteomics.
title_sort exploring new proteome space combining lys n proteolytic digestion and strong cation exchange scx separation in peptide centric ms driven proteomics
work_keys_str_mv AT taouatasn exploringnewproteomespacecombininglysnproteolyticdigestionandstrongcationexchangescxseparationinpeptidecentricmsdrivenproteomics
AT mohammeds exploringnewproteomespacecombininglysnproteolyticdigestionandstrongcationexchangescxseparationinpeptidecentricmsdrivenproteomics
AT hecka exploringnewproteomespacecombininglysnproteolyticdigestionandstrongcationexchangescxseparationinpeptidecentricmsdrivenproteomics