Open AccessThe influence of glycation on a high pressure denaturation of ubiquitin
Author(s) -
Monika Kijewska,
Karolina Radziszewska,
Marta Cal,
Mateusz Waliczek,
Piotr Stefanowicz,
Zbigniew Szewczuk
Publication year - 2016
Publication title -
bioscience reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.938
H-Index - 77
eISSN - 1573-4935
pISSN - 0144-8463
DOI - 10.1042/bsr20160233
Subject(s) - glycation , denaturation (fissile materials) , chemistry , hydrogen–deuterium exchange , ubiquitin , deuterium , mass spectrometry , fructosamine , biophysics , chromatography , biochemistry , nuclear chemistry , physics , receptor , quantum mechanics , biology , gene , medicine , insulin , endocrinology
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom