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Identification of Isoforms of Aspartic Acid Residue in Peptides by 2D UV-MS Fingerprinting of Cold Ions

Abstract

We use 2D UV-MS cold-ion spectroscopy for identifications of L-Asp, D-Asp, L-isoAsp and D-isoAsp residues in a fragment peptide derived from hormon protein amylin. Relative solution concentrations of all four isoforms in an equimolar quaternary mixture have been determined within 4% error. The method demonstrates that for binary mixtures of the peptides the accuracy of 2.5% can be reached in a few-second measurements.

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Publication details

The article was received on 18 Dec 2017, accepted on 12 Jan 2018 and first published on 12 Jan 2018


Article type: Communication
DOI: 10.1039/C7AN02044A
Citation: Analyst, 2018, Accepted Manuscript
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    Identification of Isoforms of Aspartic Acid Residue in Peptides by 2D UV-MS Fingerprinting of Cold Ions

    V. Kopysov, M. V. Gorshkov and O. V. Boyarkin, Analyst, 2018, Accepted Manuscript , DOI: 10.1039/C7AN02044A

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