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Mémoire, Partim A, COLLÉGIALITÉ

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Godaux, Simon ULiège
Promotor(s) : Eppe, Gauthier ULiège
Date of defense : 22-Jan-2024 • Permalink : http://hdl.handle.net/2268.2/19973
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Title : Mémoire, Partim A, COLLÉGIALITÉ
Author : Godaux, Simon ULiège
Date of defense  : 22-Jan-2024
Advisor(s) : Eppe, Gauthier ULiège
Committee's member(s) : Matagne, André ULiège
Kune, Christopher ULiège
Far, Johann ULiège
Language : English
Keywords : [en] Capillary electrophoresis, Ion mobility, mass spectrometry, peptides, Higher order structures
Discipline(s) : Physical, chemical, mathematical & earth Sciences > Chemistry
Target public : Researchers
Professionals of domain
Institution(s) : Université de Liège, Liège, Belgique
Degree: Master en sciences chimiques, à finalité approfondie
Faculty: Master thesis of the Faculté des Sciences

Abstract

[en] Native mass spectrometry (nMS) coupled to ion mobility (IM-MS) is an analytical strategy for studying
biological systems, particularly proteins and peptides, after transferring them to the gas phase.
However, can the absence of certain interactions in the gas phase compared to those in solution result
in new conformations compared to their native states? Or are ionic conformations kinetically trapped?
The aim of this work is to provide some answers to these questions by studying peptides obtained
following trypsin digestion of a well-known protein, bovine serum albumin. The peptides derived from
this digestion were studied using two separation methods, one in the gas phase (ion mobility) coupled
with another in solution (capillary electrophoresis), which also provided information on the structural
parameters of the systems studied. Both methods were tested under different conditions (pH,
interface between the two methods, ion activation regime) to determine the influence of experimental
parameters. After analysis and interpretation of the results, it was found that despite similar
conformational distributions between the two phases for the majority of peptides. Some peptides
undergo conformational changes after desolvation.


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Author

  • Godaux, Simon ULiège Université de Liège > Master en sc. chimiques, fin. approf.

Promotor(s)

Committee's member(s)

  • Matagne, André ULiège Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines
    ORBi View his publications on ORBi
  • Kune, Christopher ULiège Université de Liège - ULiège > Département de chimie (sciences) > Laboratoire de spectrométrie de masse (L.S.M.)
    ORBi View his publications on ORBi
  • Far, Johann ULiège Université de Liège - ULiège > Département de chimie (sciences) > Chimie analytique inorganique
    ORBi View his publications on ORBi
  • Total number of views 37
  • Total number of downloads 5










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