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- Publisher Website: 10.1016/j.jasms.2005.05.001
- Scopus: eid_2-s2.0-23844455276
- PMID: 16023365
- WOS: WOS:000231646500014
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Article: Experimental and theoretical investigations of the loss of amino acid side chains in electron capture dissociation of model peptides
Title | Experimental and theoretical investigations of the loss of amino acid side chains in electron capture dissociation of model peptides |
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Authors | |
Issue Date | 2005 |
Citation | Journal of the American Society for Mass Spectrometry, 2005, v. 16, n. 9, p. 1523-1535 How to Cite? |
Abstract | Loss of side chains from different amino acid residues in a model peptide framework of RGGGXGGGR under electron capture dissociation conditions were systematically investigated, where X represents one of the twenty common amino acid residues. The α-carbon radical cations initially formed by N-C α cleavage of peptide ions were shown to undergo secondary dissociation through losses of even-electron and/or odd-electron side-chain moieties. Among the twenty common amino acid residues studied, thirteen of them were found to lose their characteristic side chains in terms of odd-electron neutral fragments, and nine of them were found to lose even-electron neutral side chains. Several generalized dissociation pathways were proposed and were evaluated theoretically with truncated leucine-containing models using ab initio calculations at B3-PMP2/6-311 ++ G(3df,2p)//B3LYP/6-31 ++ G(d,p) level. Elimination of odd-electron side chain was associated with the initial abstraction of the hydrogen from the α-carbon bearing the side chain by the N-terminal α-carbon radical. Subsequent formation of α-β carbon-carbon double bond leads to the elimination of the odd-electron side chain. The energy barrier for this reaction pathway was 89 kJmol -1. This reaction pathway was 111 kJmol -1 more favorable than the previously proposed pathway involving the formation of cyclic lactam. Elimination of even-electron side chain was associated with the initial abstraction of the γ-hydrogen from the side chain by the N-terminal α-carbon radical. Subsequent formation of β-γ carbon-carbon double bond leads to the elimination of the even-electron side chain and the migration of the radical center to the α-carbon. The energy barrier for this fragmentation reaction was found to be 50 kJmol -1. © 2005 American Society for Mass Spectrometry. |
Persistent Identifier | http://hdl.handle.net/10722/206252 |
ISSN | 2023 Impact Factor: 3.1 2023 SCImago Journal Rankings: 0.725 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Fung, Yi Man Eva | - |
dc.contributor.author | Chan, Tak Wah Dominic | - |
dc.date.accessioned | 2014-10-22T01:25:31Z | - |
dc.date.available | 2014-10-22T01:25:31Z | - |
dc.date.issued | 2005 | - |
dc.identifier.citation | Journal of the American Society for Mass Spectrometry, 2005, v. 16, n. 9, p. 1523-1535 | - |
dc.identifier.issn | 1044-0305 | - |
dc.identifier.uri | http://hdl.handle.net/10722/206252 | - |
dc.description.abstract | Loss of side chains from different amino acid residues in a model peptide framework of RGGGXGGGR under electron capture dissociation conditions were systematically investigated, where X represents one of the twenty common amino acid residues. The α-carbon radical cations initially formed by N-C α cleavage of peptide ions were shown to undergo secondary dissociation through losses of even-electron and/or odd-electron side-chain moieties. Among the twenty common amino acid residues studied, thirteen of them were found to lose their characteristic side chains in terms of odd-electron neutral fragments, and nine of them were found to lose even-electron neutral side chains. Several generalized dissociation pathways were proposed and were evaluated theoretically with truncated leucine-containing models using ab initio calculations at B3-PMP2/6-311 ++ G(3df,2p)//B3LYP/6-31 ++ G(d,p) level. Elimination of odd-electron side chain was associated with the initial abstraction of the hydrogen from the α-carbon bearing the side chain by the N-terminal α-carbon radical. Subsequent formation of α-β carbon-carbon double bond leads to the elimination of the odd-electron side chain. The energy barrier for this reaction pathway was 89 kJmol -1. This reaction pathway was 111 kJmol -1 more favorable than the previously proposed pathway involving the formation of cyclic lactam. Elimination of even-electron side chain was associated with the initial abstraction of the γ-hydrogen from the side chain by the N-terminal α-carbon radical. Subsequent formation of β-γ carbon-carbon double bond leads to the elimination of the even-electron side chain and the migration of the radical center to the α-carbon. The energy barrier for this fragmentation reaction was found to be 50 kJmol -1. © 2005 American Society for Mass Spectrometry. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of the American Society for Mass Spectrometry | - |
dc.title | Experimental and theoretical investigations of the loss of amino acid side chains in electron capture dissociation of model peptides | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/j.jasms.2005.05.001 | - |
dc.identifier.pmid | 16023365 | - |
dc.identifier.scopus | eid_2-s2.0-23844455276 | - |
dc.identifier.volume | 16 | - |
dc.identifier.issue | 9 | - |
dc.identifier.spage | 1523 | - |
dc.identifier.epage | 1535 | - |
dc.identifier.isi | WOS:000231646500014 | - |
dc.identifier.issnl | 1044-0305 | - |