CPSA Shanghai 2013
Reviving Pharmaceutical R&D with Translational Science, Regulatory Efficiency, and Innovative Models
April 24 - 27, 2013
Renaissance Shanghai Pudong Hotel
Shanghai, China
Peptide and Protein Characterization Workshop
Wednesday, April 24, 2013
1:00 pm - 4:00 pm
Shanghai Institute of Materia Medica
Yisheng Hall, Bldg 1, CAS. 555 Zu-Chong-Zhi Road
Pudong New District, Shanghai
Workshop co-chairs:
Nathan A. Yates, University of Pittsburgh
Gary A. Valaskovic, New Objective, Inc.
Min-Jia Tan, Shanghai Institute of Materia Medica, CAS
Data Independent Acquisition in Proteomics Analysis
Nathan A. Yates, Ph.D
Scientific Director, Biomedical Mass Spectrometry Center, University of Pittsburgh
Traditionally, shotgun proteomics experiments have used data dependent acquisition wherein the mass spectrometer performed an initial scan of precursor ions and selected a sampling of those ions for fragmentation and generation of MS/MS spectra. Because instruments can’t scan quickly enough to acquire all the precursors entering at a given moment, however, many ions – particularly low-abundance ions – are never selected for MS/MS fragmentation and so are not detected. In DIA, the mass spec selects broad m/z windows and fragments all precursors in that window, allowing the machine to collect MS/MS spectra on all ions in a sample. In combining qualitative and quantitative proteomics analysis, DIA techniques have been employed by a number of proteomics researchers using a variety of different platforms.
Nanospray Technologies for Proven Characterization with Established and Emerging Technologies
Gary A. Valaskovic, Ph.D.
President & CEO, New Objective Inc.
Traditionally, shotgun proteomics experiments have used data dependent acquisition wherein the mass spectrometer performed an initial scan of precursor ions and selected a sampling of those ions for fragmentation and generation of MS/MS spectra. Because instruments can’t scan quickly enough to acquire all the precursors entering at a given moment, however, many ions – particularly low-abundance ions – are never selected for MS/MS fragmentation and so are not detected. In DIA, the mass spec selects broad m/z windows and fragments all precursors in that window, allowing the machine to collect MS/MS spectra on all ions in a sample. In combining qualitative and quantitative proteomics analysis, DIA techniques have been employed by a number of proteomics researchers using a variety of different platforms.
Multi PTM Analysis on LTQ-Orbitrap Hybrid Mass Spectrometer
Min-Jia Tan, Ph.D.
Shanghai Institute of Materia Medica, CAS
Protein translational modifications (PTMs) of proteins are complex and fundamental mechanisms of cellular regulation, and have been associated with almost all known cellular pathways and disease processes. Among them, phosphorylation, ubiquitination, acetylation have been by far the most well-characterized. With the advancement of high-resolution mass spectrometry (MS) technologies, MS-based have been the fundamental tool for detecting, mapping and quantifying protein covalent modifications, and large-scale modification-specific proteomics studies. Here we describe and applications of MS-based strategies and bioinformatics tool used to detect common PTMs, map protein modification sites, quantitive global profiling of PTMs, noting the advantages and drawbacks of different approaches.
CPSA Shanghai - Where Technology and Solutions Meet. Where East Meets West.