Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase.
We introduce a method for sequencing peptides by mass spectrometry using a metalloendopeptidase that cleaves proteins at the amino side of lysine (Lys-N). When analyzed by electron transfer dissociation (ETD)-based mass spectrometric sequencing, Lys-N-digested peptides that contain a single lysine r...
Main Authors: | , , , |
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Format: | Journal article |
Language: | English |
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2008
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_version_ | 1797087996656222208 |
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author | Taouatas, N Drugan, M Heck, A Mohammed, S |
author_facet | Taouatas, N Drugan, M Heck, A Mohammed, S |
author_sort | Taouatas, N |
collection | OXFORD |
description | We introduce a method for sequencing peptides by mass spectrometry using a metalloendopeptidase that cleaves proteins at the amino side of lysine (Lys-N). When analyzed by electron transfer dissociation (ETD)-based mass spectrometric sequencing, Lys-N-digested peptides that contain a single lysine residue produce spectra dominated by c-type fragment ions, providing simple ladders for sequence determination. This method should be a valuable strategy for de novo sequencing and the analysis of post-translational modifications. |
first_indexed | 2024-03-07T02:43:34Z |
format | Journal article |
id | oxford-uuid:ab445972-f979-460d-a145-65737ba0407e |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T02:43:34Z |
publishDate | 2008 |
record_format | dspace |
spelling | oxford-uuid:ab445972-f979-460d-a145-65737ba0407e2022-03-27T03:20:49ZStraightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ab445972-f979-460d-a145-65737ba0407eEnglishSymplectic Elements at Oxford2008Taouatas, NDrugan, MHeck, AMohammed, SWe introduce a method for sequencing peptides by mass spectrometry using a metalloendopeptidase that cleaves proteins at the amino side of lysine (Lys-N). When analyzed by electron transfer dissociation (ETD)-based mass spectrometric sequencing, Lys-N-digested peptides that contain a single lysine residue produce spectra dominated by c-type fragment ions, providing simple ladders for sequence determination. This method should be a valuable strategy for de novo sequencing and the analysis of post-translational modifications. |
spellingShingle | Taouatas, N Drugan, M Heck, A Mohammed, S Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. |
title | Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. |
title_full | Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. |
title_fullStr | Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. |
title_full_unstemmed | Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. |
title_short | Straightforward ladder sequencing of peptides using a Lys-N metalloendopeptidase. |
title_sort | straightforward ladder sequencing of peptides using a lys n metalloendopeptidase |
work_keys_str_mv | AT taouatasn straightforwardladdersequencingofpeptidesusingalysnmetalloendopeptidase AT druganm straightforwardladdersequencingofpeptidesusingalysnmetalloendopeptidase AT hecka straightforwardladdersequencingofpeptidesusingalysnmetalloendopeptidase AT mohammeds straightforwardladdersequencingofpeptidesusingalysnmetalloendopeptidase |