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DTSTAMP:20260414T025813
DTSTART:20151125T110000
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DTEND:20151125T123000
URL:https://murmitoyen.com/events/vanille/udem/detail/624076
LOCATION:Université de Montréal - Pavillon Roger-Gaudry\, 2900\, chemin d
 e la Tour\, Montréal\, QC\, Canada\, H3T 1J6
SUMMARY:Conférence du Professeur Roberto Chica (Ottawa)
DESCRIPTION:Titre : Multistate Computational protein Design with Backbone E
 nsembles: Applications in Protein Engineering and Systems Biology.Endroit 
 : Pavillon Roger-Gaudry\, salle G-815 à 11 hHôte : Professeure Joelle Pe
 lletier
\nLa conférence sera prononcée (en anglais) par le professeur Ro
 berto Chica\, du Département de chimie de l'Université d'Ottawa.
\nRésu
 mé : Computational protein design (CPD) is a useful tool for protein engi
 neers. It has been successfully applied towards the creation of proteins w
 ith increased stability\, improved binding affinity\, novel enzymatic acti
 vity\, and altered ligand specificity. Traditionally\, CPD calculations se
 arch and rank sequences using a single fixed protein backbone template in 
 an approach referred to as single-state design. Despite numerous successes
 \, singlestate design is prone to false negative predictions that result f
 rom the combined use of a single fixed backbone template and a discrete se
 t of rigid rotamers. This known artefact of single-state design leads to t
 he incorrect rejection of sequences that could have been otherwise tolerat
 ed using slightly different rotamer and backbone geometries during calcula
 tion. This fixed backbone approximation can be addressed with multistate d
 esign\, an emerging methodology in CPD that considers any number of protei
 n conformational states as inputs to calculation. Multistate design improv
 es the prediction of stable and functional proteinsequences by using backb
 one ensembles approximating conformational flexibility as input templates 
 instead of a single fixed protein structure. In this presentation\, we wil
 l show how multistate design with backbone ensembles can be successfully a
 pplied towards (1) the design of stable globular proteins with accurately 
 predicted stability\, (2) the control of protein conformational equilibriu
 m\, and (3) the discovery of substrates for an enzyme depositing posttrans
 lational modifications.
\nInformation supplémentaireAnnonce PDF de la con
 férence
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