Nos Commanditaires : IRIC 16 avril, h00 Salle S1-151 Pavillon Jean-Coutu Université de Montréal

IRIC 16 avril, h00 Salle S1-151 Pavillon Jean-Coutu Université de Montréal Christoph H. Borchers Full Professor, University of Victoria Director, UVic Genome BC Proteomics Centre Novel Approaches in Quantitative and Structural Proteomics for Clinical Research and Diagnostics Protein quantitation is essential for screening biomarker candidates for disease stratification and monitoring, and to verify and validate these biomarkers. Accurate plasma protein concentrations can be determined through a targeted, multiplexed approach involving Multiple Reaction Monitoring (MRM), in conjunction with stable isotope-labeled standard (SIS) peptides. To improve the robustness of MRMs toward the analysis of thousands of patient samples, we have developed assays using standard-flow UPLC/MRM-MS for quantitating multiple proteins (>100) in undepleted human specimen including plasma, urine and CSF. Recent developments in the modern mass spectrometry of proteins and peptides have resulted in significant progress in structural proteomics techniques for studying protein structure. A variety of protein structural questions, ranging from defining protein interaction networks to the study of conformational changes and the structure of single proteins, can be addressed using multiple mass spectrometry based structural proteomics approaches. Each technique provides specific structural information which can be used as experimental structural constraints in protein-structure modeling. Here, we describe recent developments in limited proteolysis, surface modification, hydrogen-deuterium exchange, ion mobility, and crosslinking -- all combined with modern mass spectrometric techniques -- for studying the structure of clinical relevant proteins like prion..

Our Sponsors: IRIC April 16, h00 Room S1-151 Pavillon Jean-Coutu Université de Montréal

IRIC April 16, h00 Room S1-151 Pavillon Jean-Coutu Université de Montréal Christoph H. Borchers Full Professor, University of Victoria Director, UVic Genome BC Proteomics Centre Novel Approaches in Quantitative and Structural Proteomics for Clinical Research and Diagnostics Protein quantitation is essential for screening biomarker candidates for disease stratification and monitoring, and to verify and validate these biomarkers. Accurate plasma protein concentrations can be determined through a targeted, multiplexed approach involving Multiple Reaction Monitoring (MRM), in conjunction with stable isotope-labeled standard (SIS) peptides. To improve the robustness of MRMs toward the analysis of thousands of patient samples, we have developed assays using standard-flow UPLC/MRM-MS for quantitating multiple proteins (>100) in undepleted human specimen including plasma, urine and CSF. Recent developments in the modern mass spectrometry of proteins and peptides have resulted in significant progress in structural proteomics techniques for studying protein structure. A variety of protein structural questions, ranging from defining protein interaction networks to the study of conformational changes and the structure of single proteins, can be addressed using multiple mass spectrometry based structural proteomics approaches. Each technique provides specific structural information which can be used as experimental structural constraints in protein-structure modeling. Here, we describe recent developments in limited proteolysis, surface modification, hydrogen-deuterium exchange, ion mobility, and crosslinking -- all combined with modern mass spectrometric techniques -- for studying the structure of clinical relevant proteins like prion..