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Electron transfer dissociation of melectin peptide: correlating the precursor ion structure with peptide backbone dissociations
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SYSNO ASEP 0360640 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Electron transfer dissociation of melectin peptide: correlating the precursor ion structure with peptide backbone dissociations Author(s) Moss, Ch. L. (US)
Chung, T. W. (US)
Čeřovský, Václav (UOCHB-X) RID, ORCID
Tureček, F. (US)Number of authors 4 Source Title Collection of Czechoslovak Chemical Communications. - : Ústav organické chemie a biochemie AV ČR, v. v. i. - ISSN 0010-0765
Roč. 76, č. 4 (2011), s. 295-309Number of pages 15 s. Language eng - English Country CZ - Czech Republic Keywords mass spectrometry ; peptides ; ab initio calculations Subject RIV CC - Organic Chemistry CEZ AV0Z40550506 - UOCHB-X (2005-2011) UT WOS 000289355200006 DOI 10.1135/cccc2011025 Annotation 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. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2012
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