Inducing bacterial protein recrystallization through hydrophobic and hydrophilic nanoprotrusions
Abstract
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).
S-Protein Atomic Force Microscopy Self-assembly Surface chemistry Hydrophobic interactions
Publikationen
Project staff
José Luis Toca-Herrera
Univ.Prof. Dr. José Luis Toca-Herrera
jose.toca-herrera@boku.ac.at
Tel: +43 1 47654-80311
Project Leader
01.01.2017 - 31.12.2021