History of mass spectrometry; Basics of MS instrumentation; Ionization sources-Electron Impact (EI), Chemical ionization (CI), Fast Atom Bombardment (FAB), Electrospray (ESI), Matrix Assisted Laser Desorption and Ionization (MALDI); Mass analyzers- Quadrupole, Traps (Linear trap, 3D trap, Orbitrap, Ion Cyclotron Resonance), Time-of Flight, Hybrid analyzers; Detectors- Electron multiplier, Microchannel plate; Ion mobility mass spectrometry.
Fundamental parameters of mass spectrometers- Mass accuracy, Resolution, Sensitivity; Tandem mass spectrometry; Fragmentation techniques- Collision induced dissociation (CID), Electron transfer dissociation (ETD), Electron Capture Dissociation (ECD), Post source decay (PSD), Selected Reaction Monitoring (SRM), Multiple Reaction Monitoring (MRM); MS data interpretation of biomolecules.
History of proteomics; Protein and peptide separation techniques- Electrophoresis, HPLC; Protein identification- Peptide mass finger printing, Data dependent MS/MS, Data independent MS/MS; Database search engines- Mascot, Sequest; Proteomic work-flows- In-gel digestion, In-solution digestion; Protein validation; Top-down proteomics.
Posttranslational modification analysis- Phosphorylation, Glycosylation, Disulfide bond determination.
Quantitative proteomics- Stable isotope labeled quantitation (ICAT, iTRAQ, SILAC, TMT), Label-free quantitation (emPAI, Spectral count, Ion intensity).