Linked Life Data

20138543

Source:http://linkedlifedata.com/resource/pubmed/id/20138543

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-3-30
pubmed:abstractText
Fragmentation pathways of peptide radical cations, M(+*), with well-defined initial location of the radical site were explored using collision-induced dissociation (CID) experiments. Peptide radical cations were produced by gas-phase fragmentation of Co(III)(salen)-peptide complexes [salen = N,N'-ethylenebis (salicylideneiminato)]. Subsequent hydrogen abstraction from the beta-carbon of the side-chain followed by C(alpha)-C(beta) bond cleavage results in the loss of a neutral side chain and formation of an alpha-radical cation with the radical site localized on the alpha-carbon of the backbone. Similar CID spectra dominated by radical-driven dissociation products were obtained for a number of arginine-containing alpha-radicals, suggesting that for these systems radical migration precedes fragmentation. In contrast, proton-driven fragmentation dominates CID spectra of alpha-radicals produced via the loss of the arginine side chain. Radical-driven fragmentation of large M(+*) peptide radical cations is dominated by side-chain losses, formation of even-electron a-ions and odd-electron x-ions resulting from C(alpha)-C bond cleavages, formation of odd-electron z-ions, and loss of the N-terminal residue. In contrast, charge-driven fragmentation produces even-electron y-ions and odd-electron b-ions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1879-1123
pubmed:author
pubmed:copyrightInfo
2010 American Society for Mass Spectrometry. Published by Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
511-21
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Fragmentation of alpha-radical cations of arginine-containing peptides.
pubmed:affiliation
Chemical and Materials Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, USA. Julia.Laskin@pnl.gov
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't