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Electron transfer dissociation of melectin peptide: correlating the precursor ion structure with peptide backbone dissociations
- 1.0360640 - ÚOCHB 2012 RIV CZ eng J - Journal Article
Moss, Ch. L. - Chung, T. W. - Čeřovský, Václav - Tureček, F.
Electron transfer dissociation of melectin peptide: correlating the precursor ion structure with peptide backbone dissociations.
Collection of Czechoslovak Chemical Communications. Roč. 76, č. 4 (2011), s. 295-309. ISSN 0010-0765
Grant - others:NSF(US) CHE0750048; NSF(US) CHE-0342956
Institutional research plan: CEZ:AV0Z40550506
Keywords : mass spectrometry * peptides * ab initio calculations
Subject RIV: CC - Organic Chemistry
Impact factor: 1.283, year: 2011
Electron transfer dissociation of doubly and triply charged ions from the N-terminal decapeptide of antimicrobial peptide melectin gave different distribution of fragments ions. The triply charged ions generated series of fragment ions of c and z types while electron transfer to doubly charged ions caused backbone cleavages. The most stable doubly charged ions have globular conformations.
Permanent Link: http://hdl.handle.net/11104/0198142
Number of the records: 1