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Protein Characterization and macromolecule interaction group
The group carries out identification and characterization of protein and other macromolecular complexes using affinity purification, quantitative proteomics (SILAC, label free quantitation, dimethyl labeling at the peptide level and iTRAQ) followed by mass spectrometry analysis. Identification of post-translational modifications with special emphasis on phosphoproteomics analysis is a significant effort within the laboratory. Macromolecular interactions are investigated using a combination of pull down methods to identify novel DNA-protein and RNA-protein interactions as well as Surface Plasmon Resonance (SPR) to study binding kinetics and affinities between two macromolecules. The group has extensive expertise in chromatographic separation of proteins and peptides using SEC and HPLC technology.
• Preparation of stable lines transfected with expression clone
• Transient expression of protein of interest
• Optimization of affinity purification for protein complex characterization
• Validation of protein interactions (co-immunoprecipitation, co-localization)
• Targeted and global analysis of post translational modifications (PTM enrichment)
• Quantitative/stoichiometric assessment of protein complexes using SILAC, LFQ, dimethyl labeling and iTRAQ
• Isolation and analysis of DNA/protein and RNA/protein complexes.
• Chip-MS analysis from complex isolation to mass spectrometry analysis
• Protein fractionation using HPLC and SEC, followed by western blotting or mass spec analyses
• Kinetic assessment of molecular interactions by Surface Plasmon Resonance (SPR)
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