Show simple item record

dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorOsburn, Sandra M.en_US
dc.contributor.authorOchola, Sila O.en_US
dc.contributor.authorTalaty, Erach R.en_US
dc.contributor.authorVan Stipdonk, Michael J.en_US
dc.date.accessioned2012-02-06T17:16:30Z
dc.date.available2012-02-06T17:16:30Z
dc.date.issued2008-11-01en_US
dc.identifier18449851en_US
dc.identifier9504818en_US
dc.identifier.citationJournal of mass spectrometry : JMS. 2008 Nov; 43(11): 1458-69.en_US
dc.identifier.issn1076-5174en_US
dc.identifier.urihttp://dx.doi.org/10.1002/jms.1418en_US
dc.identifier.urihttp://hdl.handle.net/10057/4328
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractThe presence and position of a single beta-alanine (betaA), gamma-aminobutyric acid (gammaABu) or epsilon-aminocaproic acid (Cap) residue has been shown to have a significant influence on the formation of b(n)+ and y(n)+ product ions from a series of model, protonated peptides. In this study, we examined the effect of the same residues on the formation of analogous [b3 - 1 + cat]+ products from metal (Li+, Na+ and Ag+)-cationized peptides. The larger amino acids suppress formation of b3+ from protonated peptides with general sequence AAXG (where X = beta-alanine, gamma-aminobutyric acid or epsilon-aminocaproic acid), presumably because of the prohibitive effect of larger cyclic intermediates in the 'oxazolone' pathway. However, abundant [b3 - 1 + cat]+ products are generated from metal-cationized versions of AAXG. Using a group of deuterium-labeled and exchanged peptides, we found that formation of [b3 - 1 + cat]+ involves transfer of either amide or alpha-carbon position H atoms, and the tendency to transfer the atom from the alpha-carbon position increases with the size of the amino acid in position X. To account for the transfer of the H atom, a mechanism involving formation of a ketene product as [b3 - 1 + cat]+ is proposed.en_US
dc.format.extent1458-69en_US
dc.language.isoengen_US
dc.publisherJohn Wiley and Sonsen_US
dc.relation.ispartofseriesJournal of mass spectrometry : JMSen_US
dc.relation.ispartofseriesJ Mass Spectromen_US
dc.sourceNLMen_US
dc.subjectResearch Support, Non-U.S. Gov'ten_US
dc.subjectResearch Support, U.S. Gov't, Non-P.H.S.en_US
dc.subject.mesh6-Aminocaproic Acid/chemistryen_US
dc.subject.meshCationsen_US
dc.subject.meshIonsen_US
dc.subject.meshMetals/chemistryen_US
dc.subject.meshPeptides/chemistryen_US
dc.subject.meshSpectrometry, Mass, Electrospray Ionization/methodsen_US
dc.subject.meshbeta-Alanine/chemistryen_US
dc.subject.meshgamma-Aminobutyric Acid/chemistryen_US
dc.titleFormation of [b3 - 1 + cat]+ ions from metal-cationized tetrapeptides containing beta-alanine, gamma-aminobutyric acid or epsilon-aminocaproic acid residuesen_US
dc.typeArticleen_US
dc.coverage.spacialEnglanden_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 2008 John Wiley & Sons, Ltd.en_US


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record