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National Repository of Grey Literature 2 records found  Search took 0.01 seconds. 
Structural characterization of selected random protein sequences with high disorder content
 Ptáčková, Barbora ; Hlouchová, Klára (advisor) ; Šilhán, Jan (referee)
An infinitesimal fraction of the practically infinite sequence space has achieved enormous functional diversity of proteins during evolution. Intrinsically disordered proteins (IDPs) which lack a fully defined three-dimensional structure are the most likely precursors to today's proteins because of their flexible conformation and functional diversity. But how have these proteins evolved into often rigid and highly specialized protein structures? This evolutionary trajectory has the greatest support in the theory of induced fold whereby the development of the structure was mediated by the interaction and coevolution of primordial unstructured proteins with different cofactors or RNA molecules. Although some random sequences from the sequence space which is not used by nature are also able to form folded proteins the more suitable candidates for evolution of structure and function appear to be random sequences with a high content of disordered which have low aggregation propensity. The selected random protein sequences with high disorder content have been structurally characterized in this work for their further use in evolutionary studies. Three artificial proteins were selected from a random-sequence library based on previous study in our laboratory. In the present work they were purified and...
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Expression and characterization of selected never-born proteins
 Šimonová, Johana ; Hlouchová, Klára (advisor) ; Pavlíček, Jiří (referee)
This bachelor thesis deals with the study of random polypeptide sequences and occurence of secondary structure in random sequence space. Sequences for experimental characterization were selected from library containing 104 random sequences on the basis of (i) either predictions of secondary structure and disorder occurence and prediciton of solubility or (ii) a completely random selection. Eight proteins studied in this thesis belong to the second option - i.e. they were selected from the in silico generated library completely randomly. First, expression and solubility was analysed for these eight proteins. In addtion, one of the proteins was selected for further analysis. The thesis involves optimization of its expression and purification as well as its detailed biophysical characterization. (In Czech) Key words: protein evolution, protein structure, random sequences
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