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UID:69de7fd9c4b24
DTSTAMP:20260414T135641
DTSTART:20150527T110000
SEQUENCE:0
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DTEND:20150527T123000
URL:https://murmitoyen.com/events/vanille/udem/detail/487062
LOCATION:Université de Montréal - Pavillon Roger-Gaudry\, 2900\, chemin d
 e la Tour\, Montréal\, QC\, Canada\, H3T 1J6
SUMMARY:Conférence Thermo Scientific avec le Professeur Albert Heck
DESCRIPTION:Titre : A Multi-Angular View at Protein Phosphorylation by Mass
  Spectrometry.Endroit : Pavillon Roger-Gaudry\, salle G-715 à 11 hHôte :
  Professeur Pierre ThibaultCette conférence sera prononcée par le Profe
 sseur Albert Heck\, titulaire de la Chaire en spectrométrie de masse biom
 oléculaire et en protéomiques associées aux département de chimie et d
 e sciences pharmaceutiques de la Utrecht University. Elle est commanditée
  par la société Thermo Scientific et sera donnée en anglais.Résumé :
  Phosphorylation of proteins directly influences their activity\, conforma
 tion\, localization\, oligomeric state and/or binding to interaction partn
 ers. Due to this wide range of outcomes\, diverse and multidimensional ana
 lyses are required to fully monitor and understand the structural and func
 tional consequences of a protein phosphorylation event. Preferably\, such 
 assays should follow both auto- and substrate-phosphorylation\, and thus m
 onitor the substrate and the kinase simultaneously. Presently\, protein ph
 osphorylation is often investigated at unconnected levels.First\, at the p
 rotein sequence level phosphoproteomics data can be gathered on site-speci
 fic phosphorylation\, the sequence motifs recognized by a kinase and possi
 ble cross-talk between different modified sites. Secondly\, kinetic bioche
 mical analysis can provide data on the reaction rates of each enzyme-subst
 rate pair\, requirements of co-factors or certain environmental conditions
  for kinase activation\, deactivation and inhibition. Thirdly\, a range of
  structural effects of the phosphorylation event can be interrogated\, for
  example changes in conformation\, oligomeric state\, protein complex form
 ation or dissociation by using structural biology methods such as NMR\, X-
 ray crystallography and electron microscopy.In this lecture I will describ
 e various (new) ways in which mass spectrometry can be of help to study th
 ese different aspects of protein phosphorylation\, thereby focusing on new
  enrichment methods\, proteases\, and fragmentation techniques of use for 
 shot-gun phosphoproteomics. Additionally\, I will describe top-down proteo
 mics\, and native mass spectrometry based technologies and how they can be
  used in direct reaction monitoring by mass spectrometry of structural and
  functional aspects of enzyme/substrate relationships.Information supplém
 entaireDépliant de la conférence
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