Programme scientifique (pdf)

Vendredi 8 mai 2015Friday, May 8th, 2015

Pavillon Alphonse-DesjardinsUniversité Laval, Québec

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15e Symposium annuel de PROTEO

PROGRAMME SCIENTIFIQUE Ouverture et bienvenue Accueil et inscription 8h15 – 18h50 Mot de bienvenue 8h55 – 19h10

Première séance : Président: Eric Marsault, Université de Sherbrooke Elizabeth A. Edwards, University of Toronto, ON, Canada

Functional Characterization of Enzymes from Microbial Communities

9h10 – 110h00

William C. Wimley, New Orleans, LA, USA Synthetic Molecular Evolution of Membrane-active Peptides

10h00 – 10h50

Pause-café, Atrium

10h50 – 11h10

Anne S. Ulrich, Karlsruhe Institute of Technology, Allemagne Transport Across Biomembranes: Molecular Tools and Machineries

11h10 – 12h00

Diner, Le Cercle 12h00 – 13h00 Les affiches peuvent être visitées sur l’heure du diner

Deuxième séance : Président: Kalle Gehring, Université McGill Erika Milczek, Merck Research Laboratories, Rahway, NJ, USA

Identification of Key Residues within the Cytochrome P450 BM-3 Reductase Domain that Facilitate "Transferable" Improvement in Catalysis

13h00 – 13h50

Conférences étudiantes

Marc-André Robert, Université Laval Livraison efficace de protéines nucléaires et cytoplasmiques via des particules pseudovirales produites avec la polyprotéine Gag du VIH-1

13h50 – 14h10

Juliana Munoz, Université McGill The MLLE domain in UBR5: a PAM2-dependant Interaction with the HECT Domain

14h10 – 14h30

James Davey, Université d'Ottawa Discovery of Substrates for a SET Domain Lysine Methyltransferase Predicted by Multistate Computational Protein Design

14h30 – 14h50

Pause-café, Atrium

14h50 – 15h10

Thomas A. Steitz, Yale University, New Haven, CT, USA From the Structure and Function of the Ribosome to New Antibiotics

15h10 – 16h00

Séance de présentation d’affiches Séance de présentation d’affiches, Atrium 16h00 – 18h00 Remise des prix pour les meilleures affiches 18h00

SCIENTIFIC PROGRAM Opening and Registration Registration 8:15 – 18:50 Welcoming Remarks 8:55 – 19:10

Plenary 1 : Chair : Eric Marsault, Université de Sherbrooke Elizabeth A. Edwards, University of Toronto, ON, Canada


9:10 – 110:00

William C. Wimley, New Orleans, LA, USA Synthetic Molecular Evolution of Membrane-active Peptides

10:00 – 10:50

Coffee-Break, Atrium

10:50 – 11:10

Anne S. Ulrich, Karlsruhe Institute of Technology, Allemagne Transport Across Biomembranes: Molecular Tools and Machineries

11:10 – 12:00

Lunch, Le Cercle 12:00 – 1:00 Posters can be viewed during lunch time

Plenary 2 : Chair : Kalle Gehring, McGill University Erika Milczek, Merck Research Laboratories, Rahway, NJ, USA

Identification of Key Residues within the Cytochrome P450 BM-3 Reductase Domain that Facilitate "Transferable" Improvement in Catalysis

1:00 – 1:50

Student Lectures Marc-André Robert, Université Laval

Livraison efficace de protéines nucléaires et cytoplasmiques via des particules pseudovirales produites avec la polyprotéine Gag du VIH-1

1:50 – 2:10

Juliana Munoz, McGill University The MLLE domain in UBR5: a PAM2-dependant interaction with the HECT domain

2:10 – 2:30

James Davey, University of Ottawa Discovery of Substrates for a SET Domain Lysine Methyltransferase Predicted by Multistate Computational Protein Design

2:30 – 2:50

Coffee-Break, Atrium

2:50 – 3:10

Thomas A. Steitz, Yale University, New Haven, CT, USA From the Structure and Function of the Ribosome to New Antibiotics

3:10 – 4:00

Poster Session Poster Session, Atrium 4:00 – 6:00 Best Poster Awards Presentation 6:00

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Conférenciers invités Keynotes

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Elizabeth A. Edwards, Emma Master, Robyn Goacher, Alexei Savchenko, Shuiquan Tang, Xiaoming Liang, Ahsan Islam, Olivia Molenda, Luz Puentes, Charles Mims, Ana Popovic, Alexander Yakunin, Tran Hai, Anatoli Tchigvintsev, Greg Brown

Department of Chemical Engineering and Applied Chemistry, University of Toronto

Metagenomes provide thousands of new microbial gene sequences, yet each new metagenome contains a large fraction of genes that have no known function, or function that is very poorly defined. The problem of poor annotation is rampant and well appreciated, yet not amenable to high throughput solutions.

Three approaches to tackle function have been initiated in our research centre: 1) functional metagenome screens; 2) enzyme assays using complex solid or industry-relevant substrates; and 3) native PAGE separation coupled to functional screening and proteomics. These examples illustrate some of the many challenges in protein function identification, but also show that significant impact is possible through both systematic and targeted assay approaches.

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Synthetic Molecular Evolution of Membrane-active Peptides

William C. Wimley

Biochemistry and Molecular biology, Tulane University School of Medicine

Membrane-active peptides have potential utility as drug-delivery vehicles and as anti-cancer, antibacterial and antiviral therapeutics. However, it has been difficult to engineer new properties into such peptides and bring them to the clinic. The paucity of explicit sequence-structure-function relationships increases the difficulty of rational design or engineering in the laboratory. Indeed, the most noteworthy feature of membrane-active peptides is the incredible diversity of both sequence and structure such that their selection pressure has been dominated by the physical chemistry of peptide membrane interactions, rather than by highly sequence-specific interactions between biomolecules. To circumvent the lack of knowledge, my laboratory has pioneered the use of rational, iterative (2nd and 3rd generation) peptide libraries along with orthogonal high throughput screening to identify, engineer and improve membrane active peptides. We call this approach “synthetic molecular evolution”. We have successfully applied this approach to find β-sheet and α-helical equilibrium pore-forming peptides with highly novel properties, to find membrane translocating peptides for drug delivery, and to find novel antimicrobial peptides with clinically useful activities. The central finding of this work is that orthogonal screening is an effective way to identify novel membrane active peptides from iterative libraries, and that peptides identified in this way reveal important sequence-structure-function relationships.

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Transport Across Biomembranes: Molecular Tools and Machineries

Anne S. Ulrich

Karlsruhe Institute of Technology

Membrane proteins are engaged in diverse transport processes of moving hydrophilic material across hydrophobic lipid bilayers, involving e.g. pore formation or more subtle catalytic mechanisms. We demonstrate here a new structural principle for the folding and self-assembly of membrane proteins, based on electrostatic interactions. In these so-called “charge zippers”, long ladders of salt bridges form between amphiphilic transmembrane segments, running all the way across the lipid bilayer. The role of this functionally important structural motif will be illustrated for two case studies with pharmaceutical and biotechnological relevance: the biofilm-inducing peptide TisB, which enables the controlled passage of protons across bacterial membranes; and the Twin-arginine translocase, which drives the export of fully folded proteins through a pore with variable diameter. The use of solid-state 19F-NMR and CD of oriented samples, amongst other techniques to eludidate such molecular structures, will be highlighted.

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Identification of Key Residues within the Cytochrome P450 BM-3 Reductase Domain that Facilitate “Transferable” Improvements in Catalysis

Erika Milczek

Process Chemistry Department, Kerck Research Laboratories, Rahway, NJ 07065, USA

Cytochrome P450 (CYPs) enzymes are heme-containing monooxygenases that are responsible for the oxidative metabolism of xenobiotics using molecular oxygen and electrons derived from NAD(P)H. This much sought after reactivity is of great interest to chemists and biologist alike as the oxidation of C-H bonds is energetically uphill, and this reactivity has little parallel in organic synthesis. Therefore, the identification of a panel of promiscuous enzymes for the direct hydroxylation of C-H bonds is of great interest to the chemical community. The CYP isolated from Bacillus megaterium, P450 BM-3, is one of the most studied CYPs for chemical synthesis due to the higher turnover numbers and faster rates of reaction demonstrated by P450 BM-3 in comparison to other wild-type CYPs. The rapid rates of hydroxylation are largely due to the fused P450-domain (heme region) and reductase-domain (diflavin-reductase) speeding up the often rate limiting electron transfer steps from the reductase to the heme center. By targeting the FMN and FAD domains by directed evolution for beneficial mutations, a collection of enzymes were identified with improved catalytic properties. This strategy was coupled with a substrate screening-tiered approach to ensure a “general” substrate cavity was maintained. This novel evolution strategy for the CYP has resulted in a range of promiscuous enzymes with higher TON resulting in up to 15-fold improvements in the hydroxylation of a wide range of substrates. Here we present the first substrate independent evolution strategy for the CYPs. This strategy suggests that rate-determining electron transfer across multiple domains and coupling efficiency are general properties that can be targeted by directed evolution resulting in rate enhancements while maintaining the promiscuous nature of the enzyme.

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From the Structure and Function of the Ribosome to New Antibiotics

Thomas A. Steitz

Department of Molecular Biophysics & Biochemistry and Department of Chemistry at Yale University, and the Howard Hughes Medical Institute, New Haven, CT (USA)

We have obtained many insights into the structural basis of ribosome function in protein synthesis from our structural studies of the large ribosomal subunit as well as the 70S bacterial ribosome, and their complexes with substrates, protein factors or antibiotics. These have elucidated the mechanism by which this ribozyme catalyzes peptide bond formation and the specificity and mode of its inhibition by antibiotics.

During the process of protein synthesis elongation, the 70S ribosome is in various conformational states bound to various factors, and the structures of these functional states are beginning to emerge. We have obtained the structure of the complex of the 70S ribosome with tRNAs and EF-G in a previously unseen compact conformation. This compact conformation of EF-G, unlike the elongated one, allows the simultaneous binding of a tRNA in the A site and EF-G. We propose that the conversion of the compact to the elongated conformations of EF-G is responsible for tRNA translocation. The structures of the 70S ribosome with the factor EF4 (LepA) with tRNA bound in the P site or in the A and P sites provide the first insights into EF4’s possible role in protein synthesis. Our recent structures of the 70S ribosome bound to either hibernation promoting factor or ribosome modulation factor show how these factors can prevent the initiation of protein synthesis, and our structure of a complex with a ribosome rescue protein (yaeJ) shows how it rescues stalled ribosomes.

The structures of some of our antibiotic complexes have been used by Rib-X Pharmaceuticals, Inc. (now Melinta Therapeutics) of New Haven to develop new potential antibiotic compounds that are effective against MRSA, one of which has successfully completed phase II clinical trials. Recently, we have determined the crystal structures of the 70S ribosome bound to two compounds that are effective against tuberculosis, capreomycin and viomycin. Since their binding site is adjacent to the binding sites of three other antibiotics that bind to the small subunit, the design of new anti-TB antibiotics by chemically combining components of the neighboring compounds may be possible.

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Conférences étudiantes Student Lectures

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Livraison efficace de protéines nucléaires et cytoplasmiques via des particules pseudovirales produites avec la polyprotéine Gag du VIH-1

Marc-André Robert1,2,3,4, Rénald Gilbert2,3,5, Bruno Gaillet1,3,4

1Université Laval, 2CNRC-NRC, 3Réseau Thécell, 4PROTEO, 5McGill University

L’expression de la polyprotéine Gag des rétrovirus est suffisante pour induire la formation de particules pseudovirales (PPV). Une modification post-traductionnelle cible la polyprotéine à la membrane plasmique permettant son incorporation dans les PPV par bourgeonnement cellulaire. Suite au bourgeonnement, Gag est normalement clivée par la protéase rétrovirale qui libère des protéines à fonction structurale. Une approche originale consiste à fusionner Gag avec différentes protéines pour les incorporer dans les PPV et les livrer dans les cellules par la suite. Dans cette étude, Gag du VIH-1 a été fusionnée à la protéine fluorescente verte (GFP) et à deux facteurs de transcription : un transactivateur chimérique (cTA) et un facteur de reprogrammation cellulaire (KLF4). Les PPV ont été produites par transfection dans une lignée stable (293SF-pacLV) qui exprime la protéase virale et la protéine G du VSV (VSVg) sous contrôle inductible. Les niveaux de la protéase et de VSVg ont été optimisés par transfection. Les PPV ont été complexées avec du polybrène avant la transduction de cellules HEK293. Avec les PPV-Gag-GFP, une efficacité de transduction de plus de 90% a été observée par microscopie. Deux pools stables, exprimant la GFP sous le contrôle d’un promoteur spécifique au cTA (CR5) ou à KLF4, ont été générés avec des vecteurs lentiviraux. La transduction des cellules CR5-GFP avec les PPV-Gag-cTA a fortement activé le gène rapporteur (365 fois par rapport au contrôle). Étrangement, la transduction avec les PPV-Gag-KLF4 n’a pas activé le promoteur spécifique à KLF4 dans le second pool. Des données obtenues par transfection ont démontrées que la fusion de Gag inhibait l’activité de KLF4. L’ajout du domaine d’activation de VP16 a permis d’augmenter l’activité de KLF4 d’environ 200 fois. L’habilité des PPV-Gag-VP16KLF4 pour activer la transcription est présentement à l’étude. En résumé, les PPV produites avec Gag du HIV-1 peuvent livrer des protéines cytoplasmiques et nucléaires. La plateforme développée s’avérerait très pratique pour la reprogrammation cellulaire dans le cadre la thérapie cellulaire de la myopathie de Duchenne.

Organismes subventionnaires : IRSC, Réseau Thécell, Regroupement PROTEO

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The MLLE domain in UBR5: a PAM2-dependent interaction with the HECT Domain

Juliana Muñoz, Edna Matta-Camacho, Guennadi Kozlov, Kalle Gehring

Faculty of Medicine, Department of Biochemistry, McGill University

Ubiquitination is one of the most abundant post-translational modifications in eukaryotic cells. It regulates protein degradation, protein–protein interactions and subcellular localization. This process is carried out by a complex cascade of reactions catalyzed by activating (E1), conjugating (E2), and ligating (E3) enzymes. E3 ubiquitin ligases display a high degree of specificity towards its substrates and catalyze the attachment of ubiquitin to the target protein. UBR5, also known as EDD, belongs to the HECT-type family of E3 ubiquitin ligases. It mediates ubiquitination of β-catenin, TopBP1, TERT, PEPCK, Paip2, ATMIN, among others, suggesting its role as an effector in cell cycle progression and DNA damage response in mammals. UBR5 consists of a N-terminal UBA domain, a zinc finger-like UBR-box, a domain highly homologous to the C-terminal domain of poly(A)-binding protein (MLLE), and a HECT domain. Remarkably, only two proteins in eukaryotic cells contain a MLLE domain, PABP and UBR5. In PABP, MLLE is a peptide-binding domain that recognizes effectors of translation initiation that display a conserved PAM2 (for PABP-interacting motif 2) sequence. However, it is still unclear what is the role of the MLLE domain in UBR5, especially in relation to the regulation of the ubiquitin ligase activity. In the present study, we determined the crystal structure of the MLLE domain of UBR5 in complex with the PAM2 peptide from Paip1. The structure explains overlapping PAM2 specificity by MLLE from UBR5 and PABP. We reveal a novel intra-molecular interaction in a HECT-type E3 ubiquitin ligase involving the MLLE domain and the HECT domain of UBR5. This interaction is mediated by the recognition of a PAM2-like sequence in the N-terminal lobe of the HECT domain. Our results suggest a regulatory role of the MLLE domain in the catalytic activity of UBR5 beyond binding of PAM2-containing substrates. A better understanding of PAM2 recognition by UBR5 will help in the identification of novel physiological partners and provide insight into the potential competition between UBR5 and PABP for shared binding partners. With this study we hope to contribute to the understanding of UBR5 function and its relationship with a higher network of biological processes in the cell.

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Discovery of Substrates for a SET Domain Lysine Methyltransferase Predicted by Multistate Computational Protein Design

James Davey1,2,4, Sylvain Lanouette3,4, Jean-Francois Couture 3,5, Roberto Chica1,2,5

1Department of Chemistry, University of Ottawa

2Centre for Catalysis Research and Innovation, University of Ottawa

3Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of Ottawa

4Co-first Authors

5Co-corresponding Authors

Lysine methylation is a prevalent posttranslational modification (PTM) associated with several critical cellular processes. However, its relatively low abundance and chemically inert nature hinder its detection by current proteomics methods. To facilitate the identification of substrates for the SET domain methyltransferase SMYD2, we developed a computational protein design (CPD) framework for the prediction of PTM enzyme substrate recognition motifs. This framework utilizes multistate design (MSD), an emerging methodology in CPD involving the evaluation of substitution tolerance in the context of an ensemble of peptide-protein structures. The SMYD2 substrate recognition motif predicted by MSD was found to be in excellent agreement with SPOT peptide array experiments. Comprehensive motif based searches and mutational analysis allowed for the identification of four previously unknown substrates of SMYD2. These results confirm that SMYD2 methylates substrates bearing the [LFM]-1-K*-[AFYMSHRK]+1-[LYK]+2 recognition motif.

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Présentations d'affiches Poster presentations

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1. Effet du calcium et des lipides sur la recoverine, une neuroprotéine sensible au calcium (NCS) : Étude par spectroscopie infrarouge et de résonance magnétique nucléaire à l’état solide

Kim Potvin-Fournier1,2,3,4,5,6, Thierry Lefèvre1,4,5,6, Audrey Picard-Lafond1,4,5,6, Catherine Marcotte1,4,5,6, Melanie Schneider2, Geneviève Valois-Paillard1,2,3,4,5,6, Line Cantin2,3,4, Christian Salesse2,3,4, Michèle Auger1,4,5,6

1Département de chimie, Université Laval, 2Département d'ophtalmologie, Université Laval 3CUO-Recherche, Centre de recherche du CHU de Québec, Hôpital du Saint-Sacrement, CHU de Québec, 4PROTEO, Université Laval, 5Centre de recherche sur les matériaux avancés, Université Laval, 6Centre québécois sur les matériaux fonctionnels, Université Laval

2. Experimental evolution to generate context-dependent compensatory solutions for loss-of-function diseases

Marie Filteau1, Véronique Hamel1, Isabelle Gagnon-Arsenault1, Christian Landry1

1Université Laval

3. Fluorinated NMR Probes for the Study of Membrane Topology: Monofluorinated Dimyristoylphosphatidylcholine lipid membranes.

Marie-Claude Gagnon1,2, Erik Strandberg3, Parvesh Wadhwani3, Jonathan Zerweck3, Anne S. Ulrich3, Michèle Auger2, Jean-François Paquin1

1Chaire de recherche du Canada en chimie organique et médicinale, Département de chimie, PROTEO, CCVC, Université Laval, Québec, QC

2Département de chimie, PROTEO, CERMA, CQMF, Université Laval, Québec, QC

3Karlsruhe Institute of Technology (KIT), IBG-2, Karlsruhe, Germany

4. Development of a novel therapeutic tool against MLL1-related leukemia

John Haddad1

1University of Ottawa

5. Towards the Synthesis of Monofluoroalkene-based Dipeptide Isosteres

Myriam Drouin1, Audrey Gilbert1, Jean-François Paquin1

1Canada Research Chair in Medicinal and Organic Chemistry, PROTEO, CGCC, Chemistry Department, Université Laval, Québec, QC, Canada, G1V 0A6

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6. Two different proteins encoded in the same gene promote mitochondrial fission

Annie Roy1, Benoit Vanderperre1, Julie Motard1, Jean-François Jacques1, Xavier Roucou1

1Université de Sherbrooke

7. The multicoding potential of GPCRs genes

Maxime Gagnon1, Julie Motard1, Jean-François Jacques1, Fernand Gobeil1, Xavier Roucou1


8. Caractérisation de la protéine ChuY de la voie d’acquisition de l’hème chez E. coli O157:H7

Gabrielle Labrie1, Manon Couture1

1Université Laval

9. Conformational exchange experienced by free and ligand-bound xylanase B2 from Streptomyces lividans 66

Nhung Nguyen1, Donald Gagné1, Louise Roux1, Jean-Francois Couture 2, Pratul Argawal3, Nicolas Doucet1

1INRS-Institut Armand-Frappier, Université du Québec, 2Universite d'Ottawa, 3Oak Ridge National Laboratory

10. Acetylation of PCNA sliding surface differentially regulates distinct DNA polymerases to promote genome stability

Pierre Billon1, Jian Li2, Jean-Philippe Lambert3, Anne-Claude Gingras3, Alain Verreault4, Tomohiko Sugiyama2, Jacques Côté1

1Université Laval, 2Ohio University, 3University of Toronto, 4Université de Montréal

11. Structural and functional characterization of novel proteins from the oral cavity

Aurélien Fouillen1, Rima Wazen1, Pierre Moffatt2, Christian Baron1, Jurgen Sygusch1, Antonio Nanci1

1Université de Montréal, 2Shriners Hospital for Children, McGill University

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12. Identification of candidate mimicry proteins involved in parasite-driven phenotypic changes

Francois Olivier Hebert1, Luke Phelps2, Irene Samonte2, Mahesh Panchal2, Stephan Grambauer3, Iain Barber3, Martin Kalbe2, Christian Landry1, Nadia Aubin-Horth1

1Universite Laval, 2Max Planck Institute for Evolutionary Biology, 3University of Leicester

13. Surexpression et purification de la RGS9-1 Anchor Protein (R9AP) sans segment transmembranaire

Sarah Bernier1,2,3, Habib Horchani 1,2,3, Line Cantin1,2,3, Christian Salesse1,2,3

1Université Laval, 2CUO-recherche, Centre de recherche du CHU de Québec, 3Regroupement stratégique PROTEO

14. L’analyse d'un réseau métabolique d'adipocyte dans l'analyse du métabolisme des lipides en lien avec le développement du diabète de type 2

Thierry Chénard1, André Carpentier2, André Tchernof3, Rafael Najmanovich1

1Département de Biochimie, FMSS, Université de Sherbrooke

2Département de Médecine, Services d'Endocrinologie, FMSS, Université de Sherbrooke

3Département des Sciences des Aliments et Nutrition, FSAA, Université Laval

15. Fusion to green fluorescence protein provides a novel intracellular probe of the heme status of a heme peroxidase

Samaneh Dastpeyman1, Meena Kathiresan 1, Ann English1, Gonzalo Cosa2

1Concordia University, 2McGill University

16. Investigating protein-protein interactions involved in mitochondrial heme trafficking

Alan de Aguiar Lopes1, Dorival Martins1, Ann English1

1Concordia University

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17. Cell surface glycosaminoglycans mediate plasma membrane adsorption of cationic peptide hormones: cellular and biophysical characterization

Armelle Tchoumi Neree1,2, Mathieu Laporte-Wolwertz1,2, Phuong Trang Nguyen1,2, Steve Bourgault1,2

1Université du Québec à Montréal, 2Pharmaqam

18. Analysis, validation and improvement of a Clostrdium difficile metabolic network and its use for drug-discovery.

Mathieu Larocque1, Louis-Charles Fortier1, Rafael Najmanovich1


19. Evolution of Protein Dynamics in ECP Homologues

David Bernard1, Donald Gagné1, Carol-Anne Villeneuve1, Nicolas Doucet1

1INRS-Institut Armand-Frappier

20. Effet des mutations impliquées dans les dystrophies de la rétine sur la structure et l’activité de la lécithine rétinol acyltransférase

Line Cantin1,2,3, Habib Horchani 1,2,3, Stéphane Gagné1,3, Christian Salesse1,2,3

1Université Laval, 2Cuo-Recherche, Centre de recherche du CHU de Québec, 3Regroupement stratégique PROTEO

21. Characterization of functionally-relevant, co-evolving residue sectors in the Ribonuclease A family

Chitra Narayanan1, Kimberly Reynolds2, Rama Ranganathan2, Nicolas Doucet1

1INRS-Université du Québec, 2University of Texas Southwestern Medical Center

22. Influence of 2’ O Modifications on the Stability of Parallel Stranded Adenosine Duplexes

William Copp1, Alexey Denisov1, Anne M. Noronha1, Nozhat Safaee2, Kalle Gehring2, Christopher J. Wilds1

1Concordia University, 2McGill University

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23. La caspase-7 utilise un exosite pour interagir avec PARP-1

Alexandre Desroches1, Dave Boucher1, Eric Marsault1,2, Jean-Bernard Denault1

1Université de Sherbrooke, 2IPS

24. Engineering of D-amino acid aminotransferase mutants with increased activity towards aromatic D-amino acids

Curtis J.W. Walton1,2,4, Janet E.B. Barber1,2,4, Alexa Mouawad1,2,4, Jean-Francois Couture1,3, Roberto A. Chica1,2,4

1University of Ottawa, 2Department of Chemistry, 3Department of Biochemistry, Microbiology, and Immunology, 4Centre for Catalysis Research and Innovation

25. A novel approach to disrupt the homodimeric structure of galectin-7 and its pro-apoptotic function on T-lymphocytes

Maria Claudia Vladoiu1, Marilyne Labrie1, Myriam Létourneau1, Philippe Egesborg1, Donald Gagné1, Étienne Billard1, Andrée-Anne Grosset1, Nicolas Doucet1, David Chatenet1, Yves St-Pierre1


26. Preparation and Biophysical Studies of Interstrand Cross-Linked DNA Duplexes

Lauralicia Sacre1, Gang Sun1, Christopher J. Wilds1


27. Caractérisation de l’interactome nucléaire des protéines adaptatrices NCK1 et NCK2

Noémie Lavoie1,2,4, Kévin Jacquet1,2,4, Nicolas Bisson1,2,3,4

1PROTEO, 2Centre de Recherche sur le Cancer

3Département de biologie moléculaire, biochimie médicale et pathologie de l'Université Laval 4Division Oncologie, Centre de Recherche du Centre Hospitalier Universitaire (CHU) de Québec

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28. Negative phosphoregulation of protein interaction domains by tyrosine kinase receptors

Ugo Dionne1,2,4, François Chartier1,4, Donald Gagné1,5, Michel Tremblay4, David Chatenet1,5, Nicolas Doucet1,5, Nicolas Bisson1,2,3,4

1PROTEO, 2Centre de recherche sur le cancer, Université Laval 3Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval 4CHU de Québec, division oncologie, 5INRS-Institut Armand-Frappier

29. Synthesis and growth inhibition activity of novel substituted pyrimidine derivatives bearing a sulfamide group

Carole-Anne Lefebvre1, Elsa Forcellini1, Sophie Boutin1, René C.-Gaudreault1,2, Jacques Lacroix2, Patrick Lagüe1, Patrick Mathieu1,3, Jean-François Paquin.1,4

1Université Laval, 2Centre de recherche du CHU de Québec

3Institut universitaire de cardiologie et de pneumologie de Québec

4Chaire de recherche du Canada en chimie organique et médicinale

30. Études structurale et fonctionnelle de cytochromes P450 intervenant dans la biosynthèse de la tiacumicine B, un antibiotique contre Clostridium difficile

Loreleï Masselot-Joubert1, Jérémie Hamel1, Xavier Murphy Després1, Julie Barma1, Jean-Baptiste Duvignaud1, Changesheng Zhang2, Rong Shi1

1Université Laval, 2South China Sea Institute of Oceanology, Chinese Academy of Sciences

31. Peptidomimetic inhibition of host serine proteases as a treatment against influenza

Pierre-Luc Boudreault1, Éloïc Colombo1, Pallavi Thakur1, Émilie Gravel1, Isabelle Marois1, Antoine Désile1, Dominic Cliche1, Baptiste Planc1, Martin Richter1, Catherine St-Georges1, Éric Marsault1, Richard Leduc1


32. Biophysical Characterization of the b-HLH-LZ of deltaMax

Loïka Maltais1, Cynthia Tremblay1, Mikaël Bédard1, Martin Montagne1, Pierre Lavigne1

1Département de Biochimie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke

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33. Élaboration d’un procédé enzymatique économique pour la production d’acides gras oméga hydroxylé

Thierry Vincent1, Alain Garnier1, Bruno Gaillet1

1Université Laval

34. Analyse protéomique de la spécificité des protéines adaptatrices NCK1 et NCK2

Kévin Jacquet1,2,4, Ugo Dionne1,2,4, Nicolas Bisson1,2,3,4

1PROTEO, 2Centre de Recherche sur le Cancer

3Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval 4Division Oncologie, Centre de Recherche du Centre Hospitalier Universitaire (CHU) de Québec

35. Studies on Synthetic Membrane Perturbing Peptides Incorporating Crown-Ethers by Oriented Circular Dichroism

Pierre-Alexandre Paquet-Côté1, François Otis1, Jochen Bürck2, Anne Ulrich2, Normand Voyer1

1Département de Chimie and PROTEO, Université Laval, Québec, QC, Canada. 2Institut für Biologische Grenzflächen (IBG-2), Karlsruhe Institute of Technology, Karlsruhe, Germany.

36. Synthèse et activité in vitro d'inhibiteurs d'une ectonucléotide pyrophosphatase/phosphodiestérase de type 1 (ENPP1)

Elsa Forcellini1, Elnur Elyar Shayhidin2, Marie-Chloé Boulanger2, Ablajan Mahmut2, Carole-Anne Lefevbre1, Sophie Boutin1, Xavier Barbeau3, Patrick Lagüe3, Patrick Mathieu2, Jean-François Paquin1

1Chaire de recherche du Canada en chimie organique et médicinale, Département de chimie, PROTEO, CCVC, Université Laval, Québec

2Laboratoire d'Études Moléculaires des Valvulopathies, Département de cardiologie, Université Laval, Québec

3Département de biochimie, microbiologie et bio-informatique, Université Laval, Québec

37. Allelic variations in compensatory mutation effects across genetic backgrounds and environments

Véronique Hamel1,2,3,4, Marie Filteau1,2,3,4, Isabelle Gagnon-Arsenault1,2,3,4, Chritian R. Landry1,2,3,4

1IBIS, 2PROTEO, 3Département de Biologie, 4Université Laval

19

38. Deciphering the complex interaction network of a major drug metabolizing pathway mediated by UDP-glucuronosyltransferases.

Michèle Rouleau1, Yannick Audet-Delage1, Mélanie Rouleau1, Chantal Guillemette1

1Canada Research Chair in Pharmacogenomics, CHU de Québec Research Center and Faculty of Pharmacy, Université Laval

39. Analogues macrocycliques de la neurotensine 8-13 : Effets de la restriction conformationnelle du ligand sur la liaison et la signalisation.

Marc Sousbie1,3, Élie Besserer-Offroy1,3, Philippe Sarret1,2, Richard Leduc1,2,3, Eric Marsault1,2,3

1Université de Sherbrooke, 2IPS

3Faculté de Médecine et des Sciences de la Santé, Département de Pharmacologie, Université de Sherbrooke

40. Artificial Ion Channel Proteins Incorporating Fluorinated Amino Acids

Claudia Carpentier1, Raphaël Godbout1, François Otis1, Normand Voyer1

1Département de Chimie and PROTEO, Université Laval, Québec, QC, Canada

41. Controlling Amino Acid Conformational States using Multistate Computational Protein Design

Adam Damry1, James Davey1, Natalie Goto1, Roberto Chica1

1Université d'Ottawa

42. STRUCTURAL INSIGHTS INTO THE INTERACTION BETWEEN THE FUR FAMILY OF METALLOREGULATORS AND DNA

Sabina Sarvan1, William Lam1, Jean-François Couture1

1University of Ottawa

43. Genetic robustness: the molecular mechanisms of paralogous compensation

Caroline Berger1, Hélène Vignaud1, Guillaume Diss1, Christian R Landry1

1Université Laval - Institut de Biologie Intégrative et des Systèmes - Département de Biologie - PROTEO - Québec, Canada

20

44. Optimization and characterization of synthetic antimicrobial peptides (Optimisation et caractérisation de peptides antimicrobiens synthétiques)

Nicolas Poulin1,2, Gaëlle Simon1,2, Pierre-Alexandre Paquet-Côté1,2, Michèle Auger1,2, Normand Voyer1,2

1Université Laval, 2PROTEO

45. Des protéines enzymatiques : Synthèse d'époxydes chiraux en milieu aqueux

Christopher Bérubé1, Corinne Bouchard1, Normand Voyer1

1Département de Chimie and PROTEO, Université Laval, Québec, QC, Canada

46. MemP3: Membrane protein prediction and positioning

Andrei Tudor1, Patrick Lagüe1

1Université Laval

47. Exploring the function and evolution of proteins translated from unconventional protein coding sequences

Sondos Samandi1, Jean-François Lucier1, Michelle Scott1, Xavier Roucou1

1Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Quebec, Canada.

48. A molecular zoom for the study of interactomes

Andrée-Ève Chrétien1,2,3,5, Alexandre Dubé1,2,4, Isabelle Gagnon-Arsenault1,2,3,5, Christian Landry1,2,3,5

1Université Laval, 2Ibis, 3Département de biologie, 4Département de biochimie, 5PROTEO

49. Structure-based recombination of drug resistance enzymes: structural and functional tolerance to new dynamics in artificially-evolved enzymes

Sophie Gobeil1, Jaeok Park2, Maximilian Ebert1, Donald Gagné3, Christopher Clouthier4, Jürgen Pleiss7, Nicolas Doucet5, Albert Berghuis6, Joelle Pelletier1

1Université de Montréal, 2McGill University, 3INRS-Institut Armand-Frappier, 4University of Ottawa

5INRS-Université du Québec, 6McGill, 7Institut für Technische Biochemie

21

50. Recréer et comprendre les mécanismes allostériques à l'aide d'un modèle simple d'ADN

Carl Prévost-Tremblay1, Alexis Vallée-Bélisle1

1Université de Montréal

51. Ligand binding site prediction from molecular modeling and limited experimental results: the case of a ENPP1 allosteric inhibitor

Xavier Barbeau1, Elnur Elyar Shayhidin3, Elsa Forcellini2, Marie-Chloé Boulanger3, Jean-François Paquin2, Patrick Mathieu3, Patrick Lagüe1

1Department of Biochemistry, PROTEO, Laval University

2Canada Research Chair in Organic and Medicinal Chemistry, PROTEO, Department of Chemistry, Laval University

3Laboratoire d’Études Moléculaires des Valvulopathies (LEMV), Groupe de Recherche en Valvulopathies (GRV), Quebec Heart and Lung Institute/Research Center, Department of Surgery, Laval University

52. Hyperthermostable secondary structures in EstGtA2: Salt and pH dependence

Jessica Moisan1, Fatma Meddeb2, beauregard marc3

1Université du Québec à Trois-Rivières, 2Buckman Canada / UQTR, 3PROTEO

53. Conception et applications de nanothermomètres programmables et quantitatifs en ADN

Arnaud Desrosiers1, Gareau David1, Alexis Vallée-Bélisle1

1Université de Montréal

54. Co-Expression of Two Different Proteins from the Same Humane Mature mRNA

Maxime Beaudoin1,2,3, Jean-François Jacques1,2,3, Julie Motard1,2,3, Xavier Roucou1,2,3

1Université de sherbrooke, 2Faculty of Medicine and Healt Sciences, Dept. of Biochemistry

3Pavillon de recherche appliquée sur le cancer

22

55. Preparation of Various 2,3,3-triarylacrylic Acid Esters, a Particular Class of 1,2,2-triarylethene Compounds, using Suzuki-Miyaura Coupling Reactions

Sébastien Cardinal1, Normand Voyer1

1Université Laval, 2PROTEO

56. New insights into DNA delivery using Vesicular Stomatitis Virus-based VLP.

Mathias Mangion1,2,3, Alexandre Audy1,2,3, Igor Slivac1,2,3, Rénald Gilbert3,4, Bruno Gaillet1,2,3

1Université Laval, 2PROTEO, 3ThéCell, 4National Research Council Canada

57. Investigating laccase activity in fungal enzymatic extracts obtained by solid-state fermentation

Andres Rueda1,2,5, Clara Sánchez3, Daniel Molina2,4, Sonia Ospina1, Nicolas Doucet6

1Instituto de Biotecnología, Universidad Nacional de Colombia

2Grupo de Investigación en Bioquimica y Microbiología, Universidad Industrial de Santander, Colombia

3Escuela de Microbiología, Universidad Industrial de Santander, Colombia

4Escuela de Química, Universidad Industrial de Santander, Colombia


6INRS-Université du Québec

58. Perturbation of the conformational dynamics of an active-site loop alters enzyme activity

Donald Gagné1, Rachel L. French2, Chitra Narayanan1, Pratul K. Agarwal3,4, Miljan Simonović2, Nicolas Doucet1

1INRS-Institut Armand-Frappie, r22Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, 900 S. Ashland, Chicago, IL 60607, USA, 33Computational Biology Institute and Computer Science and Mathematics Division, Oak Ridge, TN 37831, USA

44Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, US

59. L-asparaginase immobilization strategies for immunosensing device

David M. Charbonneau1,3, Alexandra Aubé1, Natalie M. Rachel1,3, Vanessa Guerrero1, Kevin Delorme1, Jean-François Masson1, Joelle N. Pelletier1,2,3,4

1Département de Chimie, Université de Montréal, 2Département de Biochimie, Université de Montréal, 3PROTEO Network, Université Laval, 4Center for Green Chemistry and Catalysis (CCVC)

23

60. Enzymatic degradation of pulping liquors and industrial dyes

manel Ghribi1, Fatma Meddeb3, beauregard marc2

1UQTR, 2PROTEO, 3Buckman Canada / UQTR

61. Identification and optimization of inhibitors of type II R67 Dihydrofolate reductase, a trimethoprim-resistant enzyme

Jacynthe Toulouse1,3, Dominic Bastien1, Delphine Forge4, Brahm Yachnin3,5, Albert Berghuis3,5, Jean Jacques Vanden Eynde3, Joelle Pelletier1,2,3

1Département de biochimie Université de Montréal, Qc, Canada

2Département de chimie Université de Montréal, Qc, Canada

3PROTEO, the Québec Network for Research on Protein Structure, Function and Engineering,

4Laboratoire de chimie organique, Université de Mons, BELGIUM, 5Department of Biochemistry, McGill University, Montréal, Qc, Canada

62. Novel tool for xylan tracking and its industrial impacts

Vinay Khatri1, Fatma Meddeb2, marc beauregard3

1Université du Québec à Trois-Rivières, 2Buckman Canada / UQTR, 3UQTR

63. Caractérisation biophysique et biochimique d'une nouvelle lipase thermostable provenant d’une souche d’Aneurinibacillus thermoaerophilus

Ximena Zottig1, Fatma Meddeb2, marc beauregard4, beauregard marc3

1Université du Québec à Trois-Rivières, 2Buckman Canada / UQTR, 3PROTEO

4UQTR

64. Elucidating the roles of helical conformational conversion in Islet Amyloid Polypeptide amyloid formation

Carole Anne De Carufel1, Noé Quittot1, Phuong Trang Nguyen1, Steve Bourgault1

1Université du Québec à Montréal

65. Probing the pathway of lambda-6 immunoglobulin light chain amyloid formation

Mathieu Laporte Wolwertz1, Phuong Trang Nguyen1, Steve Bourgault1


24

66. Structural study of Orf47 in lactococcal phage p2 by nuclear magnetic resonance

Jérémie Hamel1,2,4, Sylvain Moineau1,3,4, Rong Shi1,4, Stephane Gagne1,2,4

1Université Laval, 2Institut de Biologie Intégrative et des Systèmes

3Groupe de Recherche en Écologie Bucale, 4PROTEO

67. Development of a purification process for Vesicular Stomatitis Virus based VLP

Juliette Champeil1,2,3, Mathias Mangion1,2,3, Rénald Gilbert2,4, Alain Garnier1,2,3, Bruno Gaillet1,2,3

1Université Laval, 2Thécell, 3PROTEO, 4National Research Council Canada

68. Crystal structure and biophysical characterization of RNase 6, a member of the human RNase A superfamily

Donald Gagné1, Jacinthe Gagnon1, Jean-François Couture2, Miljan Simonović3, Nicolas Doucet1

1Institut Armand-Frappier, INRS

2Department of Biochemistry, Microbiology and Immunology, University of Ottawa

3Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago

69. Caractérisation moléculaire de l’enzyme RhlA de Pseudomonas aeruginosa pour la synthèse de rhamnolipides d’intérêt industriel

Carlos Eduardo DulceyJordan1

1INRS, 2INRS-Université du Québec

70. New roles for old residues: rewiring the residue interaction network in RNA ligase 2

Sandrine Moreira1, Emmanuel Noutahi1, Guillaume Lamoureux2, Gertraud Burger1

1Université de Montréal, 2Université Concordia

71. Effects of non-enzymatic post-translational modifications on Islet Amyloid Polypeptide fibrillogenesis

Phuong Trang Nguyen1, Margaryta Babych1, Steve Bourgault1


25

72. Combining protein painting and directed evolution techniques to produce value-added chemicals from a microbial lipase

Yossef Lopez de los Santos1, Guillaume Brault1, Nicolas Doucet1


73. Crystal structure of a phospho-transferase protein with unusual post-translational modification

Mahder Manenda1, Laura McDonald2, Irena Ekiel2, Rong Shi1

1Institut de biologie intégrative et des systèmes (IBIS), Université Laval 2Concordia University, Montréal, Québec, Canada

74. Structures of Aminoglycoside Kinase APH(2'')-Ia Illustrate a Substrate-linked Catalytic Switch

Shane Caldwell1, Albert Berghuis1

1McGill University

75. Caractérisation structurale d’une prényltransférase impliquée dans la biosynthèse de l’hormone juvénile chez la tordeuse des bourgeons de l’épinette

Marie-Ève Picard1, Aline Barbar1,2, Catherine Béliveau2, Audrey Nisole2, Stephanie Sen3, Rong Shi1, Michel Cusson1,2

1Université Laval, 2Ressources naturelles Canada, 3The College of New Jersey

76. Structural and Functional Studies of PINK1: The first ubiquitin kinase.

Shafqat Rasool1, Kalle Gehring1, Jean-François Trempe2

1Department of Biochemistry, McGill University

2Department of Pharmacology and Therapeutics, McGill University

77. The organomercuriallyase MerB possesses unique metal-binding properties

Haytham Abdelgawwad1, Lauriane Lecoq1, Michael Stevenson2, Ahmed A. Mansour1, Kevin J. Wilkinson1, JurgenSygusch 1, Dean E. Wilcox2, James G. Omichinski1

1UdeM, 2Dartmouth College

26

78. Optimization of Semiempirical Quantum Models for the Binding of Mg2+ and Ca2+ to Proteins

Esam Orabi1, Guillaume Lamoureux1


79. Investigating the genomic bases for memory variation in yeast

Francis Rousseau-Brochu1,2,3, Alexandre K. Dubé1,2,3, Christian Landry1,2,3

1Département de Biologie, Université Laval 2Institut de Biologie intégrative et des systèmes (IBIS), Université Laval, 3PROTEO

80. Development of semiempirical models for zinc metalloproteins

Bharat Kumar Sharma1, Guillaume Lamoureux1


81. Expression, Purification, and Characterization of Aspergillus niger Aromatic Ring Monooxygenases

Justin Raiche-Moyyen1, Justin Powlowski1


Participants

Prénom Nom de famille AffiliationsHaytham Abdelgawwad UdeMSarah Melissa Jane Abraham University of MontrealLorea Alejaldre Université de MontréalYannick Audet-‐Delage Université LavalMichèle Auger Université LavalMaud AUGER Université LavalMargaryta Babych UQAMSara Banerjee Universite LavalXavier Barbeau Laval UniversityMaxime Beaudoin Université de sherbrookeMikaël Bédard Université de SherbrookeElisa Bergamin Ottawa UniversityCaroline Berger Université LavalDavid Bernard INRS -‐ IAFSarah Bernier Université LavalChristopher Bérubé Université LavalPierre Billon Université LavalNicolas Bisson Université LavalMaurice Boissinot Université LavalCorinne Bouchard Université LavalPierre-‐Luc Boudreault Université de SherbrookeMariève Boulanger Université LavalSteve Bourgault UQAMDanny Bousmail McGill UniversityYvan Boutin TransBIOTechGuillaume Brault INRS-‐Institut Armand-‐FrappierShane Caldwell McGill UniversityLine Cantin Université LavalSébastien Cardinal Université LavalClaudia Carpentier Université LavalJuliette Champeil Université LavalDavid Charbonneau Université de MontréalGuillaume Charron Université LavalFrançois Chartier CRC, Université LavalThierry Chénard Université de SherbrookeRoberto Chica University of OttawaAndrée-‐Ève Chrétien Université LavalWilliam Copp Concordia UniversityJacques Corbeil Laval UniversityAlexandre Côté Université LavalManon Couture Université LavalJean-‐Francois Couture Universite d'OttawaAdam Damry Université d'OttawaSamaneh Dastpeyman Concordia UniversityJames Davey University of OttawaAlan de Aguiar Lopes Concordia UniversityCarole Anne De Carufel Université du Québec à MontréalMaxime Déraspe Université Laval

Alexandre Desroches Université de SherbrookeArnaud Desrosiers Université de MontréalUgo Dionne Université LavalJustine Dionne Université LavalNicolas Doucet INRS-‐Université du QuébecAlain Doucet MedicagoMyriam Drouin Université LavalCaroline Dufresne Université LavalCarlos Eduardo DulceyJordan INRSMatthew Eason Université d`OttawaChris Eberlein Université LavalElizabeth A. Edwards University of TorontoPhilippe Egesborg INRS-‐Institut Armand-‐FrappierMarie Filteau Laval Universityelsa forcellini université lavalAurélien Fouillen Université de MontréalDonald Gagné INRS-‐Institut Armand-‐FrappierStephane Gagne Universite LavalMarie-‐Claude Gagnon Université LavalJacinthe Gagnon Institut Armand-‐Frappier, INRSMaxime Gagnon Université de SherbrookeIsabelle Gagnon-‐Arsenault Université LavalBruno Gaillet Université LavalAlain Garnier LavalFrancis Gaudreault Universite de SherbrookeJean-‐Antoine Gauthier Cyr Université de MontréalNikunj Gevaiya Université Lavalmanel Ghribi uqtrSébastien Giguère Université de Montréal -‐ IRICSophie Gobeil Université de MontréalRaphaël Godbout Université LavalJohn Haddad University of OttawaVéronque Hamel Université LavalJérémie Hamel Université LavalFrancois Olivier Hebert Universite LavalMathieu Hénault Université LavalJean-‐François Jacques Université de SherbrookeKévin Jacquet Université LavalVinay Khatri Université du Québec à Trois-‐RivièresWiem Kristou Laval UniversityGabrielle Labrie Université LavalPatrick Lague Université LavalClaudine Lamothe Université LavalGuillaume Lamoureux Concordia UniversityChristian Landry Université LavalJacques Lapointe Université LavalMathieu Laporte Wolwertz Université du Québec à MontréalMathieu Larocque Université de SherbrookeNoémie Lavoie Université Laval

Quoc Chon Le Université LavalCarole-‐Anne Lefebvre Université LavalThierry Lefèvre Université LavalMarie-‐Laurence Lemay Université LavalJean-‐Pascal LEPETIT-‐STOFFAES Université LavalMustapha Lhor Université LavalJérémy Loehr Université LavalYossef Lopez de los Santos Armand-‐Frappier INRS UniversityAurelien Lorin MedicagoLouis-‐André Lortie Université LavalHalim Maaroufi Université LavalOlivier Mailhot Université de MontréalLoïka Maltais Université de SherbrookeMahder Manenda Université LavalMathias Mangion université Laval -‐ PROTEO -‐ ThéCellBenjamin Martial Université LavalLoreleï Masselot-‐-‐Joubert Université LavalErika Milczek Merck Research LaboratoriesSylvain Moineau Université LavalJessica Moisan PROTEO -‐ Université du Québec à Trois-‐Rivières, PSandrine Moreira Université de MontréalLouis-‐Philippe Morency Université de SherbrookeGenevieve Morrow Université LavalCas Mosterd Université LavalJulie Motard UdSJuliana Muñoz Mcgill UniversityRafael Najmanovich Université de SherbrookeChitra Narayanan INRS-‐Université du QuébecNhung Nguyen INRS-‐Institut Armand-‐Frappier, Université du QuébecPhuong Trang Nguyen Université du Québec à MontréalAnne Noronha Concordia UniversityEsam Orabi Concordia UniversityPaméla Ouellet Université Lavaltugba nur ozturk Concordia UniversityPierre-‐Alexandre Paquet-‐Côté Université Laval -‐ PROTEOScott Pavey Université LavalJoelle Pelletier Université de MontréalVan Hau Pham Université LavalMarie-‐Ève Picard Université LavalFélix Pigeon Université du Québec à RimouskiKim Potvin-‐Fournier Université LavalNicolas Poulin Université LavalCarl Prévost-‐Tremblay Université de MontréalDaniela Quaglia Université de MontréalNoé Quittot Université Québec à MontréalJustin Raiche-‐Moyyen Concordia UniversityShafqat Rasool McGill UniversityVincent Raymond Université LavalAlexandre Raymond-‐Fleury Université Laval

Miguel Retamal Université LavalMarc-‐André Robert Université Laval -‐ CNRC-‐NRC -‐ Réseau Thécell -‐ PROTÉOXavier Roucou Université de SherbrookeMichèle Rouleau Université LavalOlivier Rousseau Université de MontréalFrancis Rousseau-‐Brochu Université LavalLouise Roux INRSVincent Roy Laval UniversityAnnie Roy Université de SherbrookeAndres Rueda INRS-‐Institut Armand-‐FrappierLauralicia Sacre Concordia UniversityChristian Salesse Université LavalSondos Samandi Université de SherbrookePrit-‐Kamal Sandhu Concordia UniversityXiaoye Sang Université LavalSabina Sarvan University of OttawaPierre-‐Yves Savard PROTEORachelle Séguin Université LavalAdnane Sellam Université Laval -‐ CHUL -‐ CHUQ RESEARCH CENTERPatrick Semana Concordia UniversityAza Sezirahiga-‐Bernard University of MontrealBharat Kumar Sharma Concordia UniversityRong Shi Université LavalMarc Sousbie Université de SherbrookeThomas A. Steitz Yale UniversityYingchao Su Laval UniversityArmelle Tchoumi Neree Université du Québec à MontréalJean-‐Francois Theriault Université Laval, Centre de recherche duJacynthe Toulouse Université de MontréalDenise Tremblay Université LavalAndrei Tudor Université LavalAnne S. Ulrich Karlsruhe Institute of TechnologyThierry Vincent Université LavalNormand Voyer Université LavalCurtis Walton University of Ottawaruixuan wang university of LavalChristopher Wilds Concordia UniversityWilliam C. Wimley Tulane UniversityXimena Zottig Université du Québec à Trois-‐Rivières

Documents

Programme scientifique (pdf)