Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/43307
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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
1097-0231
Statement of
Responsibility: 
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; Peptides; Peptide Mapping; Spectrometry, Mass, Electrospray Ionization
Description: The definitive version may be found at www.wiley.com
Provenance: Published Online: 5 Feb 2007
RMID: 0020070321
DOI: 10.1002/rcm.2872
Published version: http://www3.interscience.wiley.com/journal/114111046/abstract
Appears in Collections:Chemistry publications

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