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Author Hansen, Thomas A. ♦ Jung, Hye R. ♦ Kjeldsen, Frank
Source SpringerLink
Content type Text
Publisher Springer-Verlag
File Format PDF
Copyright Year ©2011
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Chemistry & allied sciences
Subject Keyword Electron transfer dissociation ♦ Hydrogen bonding ♦ Depsipeptides ♦ Bioinformatics ♦ Organic Chemistry ♦ Proteomics ♦ Biotechnology ♦ Analytical Chemistry
Abstract Interrogation of electron transfer dissociation (ETD) mass spectra of peptide amide-to-ester backbone bond substituted analogues (depsipeptides) reveals substantial differences in the entire backbone cleavage frequencies. It is suggested that the point permutation of backbone bonds leads to changes in the predominant ion structures by removal/weakening of specific hydrogen bonding. ETD responds to these changes by redistributing the cleavage frequencies of the peptide backbone bonds. In comparison, no distinction between depsi-/peptide was observed using collision-activated dissociation, which is consistent with a general unfolding and elimination of structural information of these ions. These results should encourage further exploration of depsipeptides for gas-phase structural characterization.
ISSN 10440305
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2011-09-15
Publisher Institution The American Society for Mass Spectrometry
Publisher Place New York
e-ISSN 18791123
Journal Journal of The American Society for Mass Spectrometry
Volume Number 22
Issue Number 11
Page Count 5
Starting Page 1953
Ending Page 1957


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Source: SpringerLink