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Inducing bacterial protein recrystallization through hydrophobic and hydrophilic nanoprotrusions

Project Leader
Toca-Herrera José Luis, Project Leader
Type of Research
Basic Research
BOKU Research Units
Institute of Biophysik
Funded by
Fonds zur Förderung der wissenschaftlichen Forschung (FWF) , Sensengasse 1, 1090 Wien, Austria
Bacterial surface layer proteins (S-layers) have the ability to build protein crystal layers with nanometer regularity on solution and many different substrates. They are currently being tested as nano-templates for different biotechnological applications. However, the (path)way in which such proteins self-assemble forming organized nanostructures is not fully understood. In this context, we propose to investigate the recrystallization of three S-layer proteins, wild type SbpA and the recombinant proteins rSbpA31–1068 and rSbpA31-918, on (molecularly controlled) hydrophobic and hydrophilic disulfides. First, we will study the adsorption kinetics and recrystallization of the three bacterial proteins. Second, we would like to find the relation between the kinetics and the physical properties of the formed protein crystal (e.g. crystal domain size, lattice parameters). Third, we would like to clarify the question of the recrystallization pathway as a function of the properties of the substrate for these bacterial proteins (which also imply to get insight about protein/substrate interactions, especially about the recognition by the protein of hydrophobic and/or hydrophilic moieties).
Polymer physics; Physical chemistry ; Biophysics; Molecular biology; Nanobiotechnology;
Hydrophobic interactions; Surface chemistry; Atomic Force Microscopy; Self-assembly; S-Protein;
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