dc.contributor | Wichita State University. Department of Chemistry | en_US |
dc.contributor.author | Osburn, Sandra M. | en_US |
dc.contributor.author | Ochola, Sila O. | en_US |
dc.contributor.author | Talaty, Erach R. | en_US |
dc.contributor.author | Van Stipdonk, Michael J. | en_US |
dc.date.accessioned | 2012-02-06T17:16:30Z | |
dc.date.available | 2012-02-06T17:16:30Z | |
dc.date.issued | 2008-11-01 | en_US |
dc.identifier | 18449851 | en_US |
dc.identifier | 9504818 | en_US |
dc.identifier.citation | Journal of mass spectrometry : JMS. 2008 Nov; 43(11): 1458-69. | en_US |
dc.identifier.issn | 1076-5174 | en_US |
dc.identifier.uri | http://dx.doi.org/10.1002/jms.1418 | en_US |
dc.identifier.uri | http://hdl.handle.net/10057/4328 | |
dc.description | Click on the DOI link below to access the article (may not be free). | en_US |
dc.description.abstract | The 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.extent | 1458-69 | en_US |
dc.language.iso | eng | en_US |
dc.publisher | John Wiley and Sons | en_US |
dc.relation.ispartofseries | Journal of mass spectrometry : JMS | en_US |
dc.relation.ispartofseries | J Mass Spectrom | en_US |
dc.source | NLM | en_US |
dc.subject | Research Support, Non-U.S. Gov't | en_US |
dc.subject | Research Support, U.S. Gov't, Non-P.H.S. | en_US |
dc.subject.mesh | 6-Aminocaproic Acid/chemistry | en_US |
dc.subject.mesh | Cations | en_US |
dc.subject.mesh | Ions | en_US |
dc.subject.mesh | Metals/chemistry | en_US |
dc.subject.mesh | Peptides/chemistry | en_US |
dc.subject.mesh | Spectrometry, Mass, Electrospray Ionization/methods | en_US |
dc.subject.mesh | beta-Alanine/chemistry | en_US |
dc.subject.mesh | gamma-Aminobutyric Acid/chemistry | en_US |
dc.title | Formation of [b3 - 1 + cat]+ ions from metal-cationized tetrapeptides containing beta-alanine, gamma-aminobutyric acid or epsilon-aminocaproic acid residues | en_US |
dc.type | Article | en_US |
dc.coverage.spacial | England | en_US |
dc.description.version | peer reviewed | en_US |
dc.rights.holder | Copyright © 2008 John Wiley & Sons, Ltd. | en_US |