dc.contributor | Wichita State University. Department of Chemistry | en_US |
dc.contributor.author | Anbalagan, Victor | en_US |
dc.contributor.author | Perera, B. A. | en_US |
dc.contributor.author | Silva, A. T. M. | en_US |
dc.contributor.author | Gallardo, A. L. | en_US |
dc.contributor.author | Barber, M. | en_US |
dc.contributor.author | Barr, J. M. | en_US |
dc.contributor.author | Terkarli, S. M. | en_US |
dc.contributor.author | Talaty, Erach R. | en_US |
dc.contributor.author | Van Stipdonk, Michael J. | en_US |
dc.date.accessioned | 2012-02-06T17:15:45Z | |
dc.date.available | 2012-02-06T17:15:45Z | |
dc.date.issued | 2002-09-01 | en_US |
dc.identifier | 12271434 | en_US |
dc.identifier | 9504818 | en_US |
dc.identifier.citation | Journal of mass spectrometry : JMS. 2002 Sep; 37(9): 910-26. | en_US |
dc.identifier.issn | 1076-5174 | en_US |
dc.identifier.uri | http://dx.doi.org/10.1002/jms.350 | en_US |
dc.identifier.uri | http://hdl.handle.net/10057/4256 | |
dc.description | Click on the DOI link below to access the article (may not be free). | en_US |
dc.description.abstract | We compared the tandem mass spectra of a range of native and acetylated Ag(+) cationized peptides to determine the influence of the derivatization step on the abundance of the [b(n) + 17 + Ag](+) product ions. Using tripeptides, the smallest for which the mechanisms to generate [b(2) - 1 + Ag](+) and [b(2) + 17 + Ag](+) products are both operative, we found that in most cases acetylation causes an increase in the abundance of the C-terminal rearrangement ion, [b(2) + 17 + Ag](+), relative to the rival N-terminal rearrangement ion, [b(2) - 1 + Ag](+). The presence of a free amino group to bind to the metal ion significantly influences the relative abundances of the product ions. We propose a mechanism for the formation of the [b(n) + 17 + Ag](+) that is based on the formation of a five-membered oxazolidin-5-one and tetrahedral carbon intermediate that may collapse to a peptide upon release of CO and an imine, aided by the fact that the ring formed during C-terminal rearrangement is both a hemiacylal and hemiaminal. We also identified an influence of amino acid sequence on the relative abundances of the [b(n) + 17 + Ag](+) and [b(n) - 1 + Ag](+) product ions, whereby bulky substituents located on the alpha-carbon of the amino acid to the C-terminal side of the cleavage site apparently promote the formation of the [b(n) + 17 + Ag](+) product over [b(n) - 1 + Ag](+) when the amino acid to the N-terminal side of the cleavage site is glycine. The latter ion is the favored product, however, when the bulky group is positioned on the alpha-carbon of the amino acid to the N-terminal side of the cleavage site. | en_US |
dc.format.extent | 910-26 | 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.title | Formation of [b(n) + 17 + Ag]+ product ions from Ag+ cationized native and acetylated peptides | en_US |
dc.type | Article | en_US |
dc.coverage.spacial | England | en_US |
dc.description.version | peer reviewed | en_US |
dc.rights.holder | Copyright © 2002 John Wiley & Sons, Ltd. | en_US |