TY - THES ID - 146493707 TI - Mémoire, Partim A, COLLÉGIALITÉ AU - Godaux, Simon AU - Eppe, Gauthier AU - Matagne, André AU - Kune, Christopher AU - Far, Johann PY - 2024 PB - Liège Université de Liège (ULiège) DB - UniCat KW - Capillary electrophoresis, Ion mobility, mass spectrometry, peptides, Higher order structures KW - Physique, chimie, mathématiques & sciences de la terre > Chimie UR - https://www.unicat.be/uniCat?func=search&query=sysid:146493707 AB - 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. ER -