ACH/HSB Mass Spectrometry of Biopolymers

Lecturer: Vladimír Havlíček
Lecture: 2 hours/week + Exercise 1 hour/week
Credits: 2
Winter semester
Form of course completion: colloquium

Capacities of mass spectrometry in biomolecular analysis, history, recent trends. Basic concepts for the interpretation of conventional and collisional mass spectra: low molecular weight organics, method per analogiam, interpretation of mass spectra of biopolymers.Standard ion sources for biomolecules (ESI, MALDI), ambient techniques (DESI, DAPCI, JeDI, DART, DAPPI, EESI, DAPPI). High-resolution analysers: cyclotron, orbitrap, UHR time-of-flight – principles, spectra, applications. Ion mobility, miniaturization, collisionally-induced dissociation, other activation techniques for biomolecules (ECD, ETD). Analysis of peptides and proteins, sample preparation, mass assignment, deconvolution, peptide fragmentation, peptide mapping, posttranslational modifications, protein conformations, molecular interactions, proteomics, protein databases. Peptide sequencing, de novo sequencing. Protein quantitation (SILAC, ICAT). MS3D approaches: hydrogen-deuterium exchange and chemical crosslinking. SELDI. Analysis of nucleotides, nucleic acids, lipids, saccharides, glycolipids.Mass spectrometry imaging and its applications to medicine. Metabolomics and proteomics in diagnosing of infectious and tumor diseases. Analysis of lipids. Practical: hands on ion cyclotron resonance mass spectrometer and MALDI-TOF/TOF. Running of own samples possible. Orientation in basic nuclear magnetic resonance and electron microscopy.