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The influence of glycation on a high pressure denaturation of ubiquitin

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 ca...

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Autores principales: Kijewska, Monika, Radziszewska, Karolina, Cal, Marta, Waliczek, Mateusz, Stefanowicz, Piotr, Szewczuk, Zbigniew
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5064455/
https://www.ncbi.nlm.nih.gov/pubmed/27612498
http://dx.doi.org/10.1042/BSR20160233
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author Kijewska, Monika
Radziszewska, Karolina
Cal, Marta
Waliczek, Mateusz
Stefanowicz, Piotr
Szewczuk, Zbigniew
author_facet Kijewska, Monika
Radziszewska, Karolina
Cal, Marta
Waliczek, Mateusz
Stefanowicz, Piotr
Szewczuk, Zbigniew
author_sort Kijewska, Monika
collection PubMed
description 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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spelling pubmed-50644552016-10-26 The influence of glycation on a high pressure denaturation of ubiquitin Kijewska, Monika Radziszewska, Karolina Cal, Marta Waliczek, Mateusz Stefanowicz, Piotr Szewczuk, Zbigniew Biosci Rep Original Papers 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. Portland Press Ltd. 2016-10-14 /pmc/articles/PMC5064455/ /pubmed/27612498 http://dx.doi.org/10.1042/BSR20160233 Text en © 2016 The Author(s) http://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Original Papers
Kijewska, Monika
Radziszewska, Karolina
Cal, Marta
Waliczek, Mateusz
Stefanowicz, Piotr
Szewczuk, Zbigniew
The influence of glycation on a high pressure denaturation of ubiquitin
title The influence of glycation on a high pressure denaturation of ubiquitin
title_full The influence of glycation on a high pressure denaturation of ubiquitin
title_fullStr The influence of glycation on a high pressure denaturation of ubiquitin
title_full_unstemmed The influence of glycation on a high pressure denaturation of ubiquitin
title_short The influence of glycation on a high pressure denaturation of ubiquitin
title_sort influence of glycation on a high pressure denaturation of ubiquitin
topic Original Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5064455/
https://www.ncbi.nlm.nih.gov/pubmed/27612498
http://dx.doi.org/10.1042/BSR20160233
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