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UID:69db73e154e80
DTSTAMP:20260412T062849
DTSTART:20170915T114500
SEQUENCE:0
TRANSP:OPAQUE
DTEND:20170915T114500
URL:https://murmitoyen.com/events/vanille/udem/detail/776471-seminaire-de-l
 etudiante-sybille-pfammatter-groupe-thibault
LOCATION:Pavillon Roger-Gaudry \, 2900\, boul. Édouard-Montpetit\, Local M
 -415\, Montréal\, QC\, Canada
SUMMARY:Séminaire de l'étudiante Sybille Pfammatter (Groupe Thibault)
DESCRIPTION:Titre : '' Advanced Proteomic analysis using high-field asymmet
 ric waveform ion mobility coupeld to mass spectrometry (FAIMS-MS) ’’
\
 nEndroit : Pavillon Roger-Gaudry\, salle G-715 à 11 h 45.
\nCette conf
 érence sera prononcée par Madame Sybille Pfammatter\, étudiante au doct
 orat du laboratoire de Pierre Thibault\, professeur au Département de ch
 imie de l'Université de Montréal.
\nRÉSUMÉ:  Sample complexity observe
 d in cell extracts places considerable demands on MS instruments to obtain
  comprehensive proteome analyses. Despite remarkable advances in MS sensit
 ivity and resolution\, the depth of proteomic analyses is often limited by
  the difficulty of sequencing low abundance peptides that are confounded w
 ith co-eluting isobaric ions and give rise to chimeric MS/MS spectra. In t
 his context\, gas phase ion separation using high field asymmetric wavefor
 m ion mobility spectrometry (FAIMS) is a useful separation technique to en
 hance peak capacity and MS sensitivity while reducing peptide co-fragmenta
 tion. We report here the application of a compact FAIMS interface coupled 
 to the newest generation of Orbitrap mass spectrometers. FAIMS enables sig
 nal to noise ratio increase by a factor of 10 to 50 enabling identificatio
 n of low abundant ions undetected with the conventional source. The additi
 onal peak capacity provided with FAIMS also alleviates the issue of peptid
 e co-fragmentation and reporter ion signal compression for isobaric labeli
 ng and provides more accurate quantitation measurements.
\nInformation sup
 plémentaireAnnonce PDF du séminaire
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