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Structural characterization of biotechnologically and medicinally important proteins.
 Filandr, František ; Man, Petr (advisor) ; Šebela, Marek (referee) ; Škultéty, Ľudovít (referee)
A large number of biological processes depends on dynamics of protein structure and specific protein-protein and protein-ligand interactions occurring under specific native conditions in or outside of cells. Standard methods for protein structure analysis like x-ray crystallography, nuclear magnetic resonance or cryo-EM are able to obtain important atomic or near- atomic resolution protein structures, however these are usually a static snapshot of protein locked in a specific conformation and mostly in non-native conditions. Structural mass spectrometry on the other hand, allows to describe protein structure dynamics, protein-protein and protein-ligand interactions and obtain inter- and intraprotein distance constraints between amino acid residues, all while working with proteins in their native conditions and needing only a fraction of sample. In this work, hydrogen/deuterium exchange mass spectrometry (HDX-MS) and classical proteomic approaches were used together with other methods to analyse biotechnologically important proteins of fungal cellulolytic system lytic polysaccharide monooxygenase (LPMO) and cellobiose dehydrogenase (CDH) as well as plant-derived photosensitizer protein LOV2 with potential use in biologically targeted photodynamic therapy. These methods allowed us to follow...
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