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Updated: Mar 15, 2026

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
Published on: June 17, 2020
The influence of glycation on a high pressure denaturation of ubiquitin
Monika Kijewska1, Karolina Radziszewska2, Marta Cal2
1Faculty of Chemistry, University of Wrocław, Wrocław 50-383, Poland monika.kijewska@chem.uni.wroc.pl.
Abstract:
The combination of deuterium-hydrogen exchange (DHX) and mass spectrometry (MS) can be used for studying a high pressure denaturation (HPD) of proteins. Herein we present the results of investigations of the influence of glycation on the HPD of ubiquitin. Application of various values of pressure causes different degrees of protein unfolding, resulting in molecules with a different number of protons available for exchange with deuterons. The dependence of this number on pressure gives information on the denaturation state of a protein. On the basis of the obtained results we can conclude that increasing number of fructosamine moieties in ubiquitin decreases the pressure required for its denaturation. It suggests that glycation moderately decreases the protein stability. The present study is the first example of application of hydrogen-deuterium exchange as a method of investigating the influence of posttranslational modification of protein on the HPD.
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