Product category:
Mass spectrometers
News Release from: Thermo Fisher Scientific (Mass Spectrometry) | Subject: LTQ XL linear ion trap mass spectrometer
Edited by the Laboratorytalk Editorial
Team on 27 February 2007
Protein and peptide analysis on ion trap
mass spec
Thermo Fisher Scientific has unveiled the Thermo Scientific LTQ XL linear ion trap mass spectrometer equipped with electron transfer dissociation (ETD)
This innovative ion fragmentation technology provides important new peptide structure information not available from conventional dissociation methods The addition of ETD to the award-winning LTQ XL linear ion trap mass spectrometer provides significant advantages for protein/peptide characterization, post-translational modification (PTM) analysis and top-down or middle-down sequencing of proteins and peptides
This article was originally published on Laboratorytalk on 12 Mar 2007 at 8.00am (UK)
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The LTQ XL with ETD option is displayed at Thermo Scientific at Pittcon 2007, being held February 26 to March 2 in Chicago, USA.
ETD technology takes advantage of the huge ion storage capacity and fast cycle times of Thermo Scientific linear ion trap Technology, allowing researchers to conduct rapid, alternating collisionally induced dissociation (CID) and ETD scanning throughout the LC/MSn analysis of complex samples, in a way that is not possible on three-dimensional ion traps.
A new version of BioWorks software streamlines the processing of ETD data.
CID and ETD spectra are searched independently, with results from both searches combined for easy comparison and sorting.
This new system provides the most complete view of a proteome possible.
The combination of LTQ XL and ETD technology produces sensitive, stable, robust ETD spectra using reagent anions generated in a CI source mounted at the back of the linear ion trap.
ETD produces C- and Z-type peptide fragment ions, complementing the Y- and B-type fragments generated during traditional CID of peptides by ion trap analysis.
This additional information allows for more complete characterisation of peptides and proteins than is possible with CID alone.
In addition, ETD technology is a uniquely powerful tool for the analysis of post-translational modifications - ETD fragmentation leaves these modifications intact, rather than causing neutral loss events commonly seen with CID analysis of phosphopeptides.
PTMs can be identified directly with a new level of confidence.
ETD is just one type of useful ion-ion reaction that can be performed; the ETD source option hardware supports multiple ion-ion reaction types, including proton transfer reaction (PTR).
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