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https://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 |
DOI: | 10.1002/rcm.2872 |
Published version: | http://www3.interscience.wiley.com/journal/114111046/abstract |
Appears in Collections: | Aurora harvest 6 Chemistry publications |
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