Document Detail


Multiple neutral loss monitoring (MNM): a multiplexed method for post-translational modification screening.
MedLine Citation:
PMID:  16443369     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Post-translational modifications of proteins are involved in determining the activity of proteins and are essential for proper protein function. Current mass spectrometric strategies require one to specify a particular type of modification, in some cases also a particular charge state of a protein or peptide that is to be studied before the actual analysis. Due to these requirements, most of the modifications on proteins are not considered in such an experiment and, thus, a series of similar analyses need to be performed to ensure a more extensive characterization. A novel scan strategy has been developed, multiple neutral loss monitoring (MNM), allowing for the comprehensive screening of post-translational modifications (PTM) on proteins that fragment as neutral losses in a mass spectrometer. MNM method parameters were determined by performing product ion scans on a number of modified peptides over a range of collision energies, providing neutral loss energy profiles and optimal collision energies (OCE) for each modification, supplying valuable information pertaining to the fragmentation of these modifications and the necessary parameters that would be required to obtain the best analysis. As the optimal collision energy was highly dependent on the type of modification and the charge state of the peptide, the MNM scan was operated with a collision energy gradient. Autocorrelation analyses identified the type of modification, and convolution mapping analyses identified the associated peptide. The MNM scan with the new collision energy parameters was successfully applied to a mixture of four modified peptides in a BSA digest. The implementation of this technique will allow for comprehensive screening of all modifications that fragment as neutral losses.
Authors:
Michael D Hoffman; Matthew J Sniatynski; Jason C Rogalski; J C Yves Le Blanc; Juergen Kast
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-01-27
Journal Detail:
Title:  Journal of the American Society for Mass Spectrometry     Volume:  17     ISSN:  1044-0305     ISO Abbreviation:  J. Am. Soc. Mass Spectrom.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-28     Completed Date:  2006-06-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9010412     Medline TA:  J Am Soc Mass Spectrom     Country:  United States    
Other Details:
Languages:  eng     Pagination:  307-17     Citation Subset:  IM    
Affiliation:
The Biomedical Research Centre, University of British Columbia, Vancouver, British Columbia, Canada.
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MeSH Terms
Descriptor/Qualifier:
Algorithms*
Gas Chromatography-Mass Spectrometry / methods*
Peptide Mapping / methods*
Peptides / analysis*,  chemistry*
Protein Processing, Post-Translational*
Spectrometry, Mass, Electrospray Ionization / methods*
Chemical
Reg. No./Substance:
0/Peptides

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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