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Type: Journal article
Title: Identification of intermolecular disulfide linkages in underivatised peptides using negative ion electrospray mass spectrometry. A joint experimental and theoretical study
Author: Bilusich, D.
Bowie, J.
Citation: Rapid Communications in Mass Spectrometry, 2007; 21(5):619-628
Publisher: John Wiley & Sons Ltd
Issue Date: 2007
ISSN: 0951-4198
Statement of
Daniel Bilusich, John H. Bowie
Abstract: The [M--H](-) ion of a symmetrical peptide containing one intermolecular disulfide linkage cleaves through the disulfide link to produce up to four fragment anions. Two of these characteristic fragments are formed by a cleavage initiated from the Cys enolate anion on the peptide backbone. The other fragment anions are formed by a cleavage directed from an anion site on the disulfide side chain. In the case of an unsymmetrical peptide containing one intermolecular disulfide, the [M--H](-) anion may cleave through the disulfide unit to give a maximum of eight cleavage anions. These fragmentations are low-energy processes as determined by theoretical calculations carried out at the HF/6-31G(d)//AM1 level of theory. Collision-induced mass spectra of the fragment anions may provide the sequence of the peptide.
Keywords: Disulfides
Peptide Mapping
Spectrometry, Mass, Electrospray Ionization
Description: The definitive version may be found at
Provenance: Published Online: 5 Feb 2007
DOI: 10.1002/rcm.2872
Published version:
Appears in Collections:Aurora harvest 6
Chemistry publications

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