Research of our group concentrates on mechanisms of protein folding and the recognition of complex carbohydrates by proteins. The model proteins we use in the majority of our studies are bacteriophage tailspike proteins (TSP). TSP are homotrimeric carbohydrate-recognition modules used by certain bacteriophages, i.e. viruses of bacteria, to attach to the lipopolysaccharide layer on the surface of their host cells. All TSP so far investigated carry an endoglycosidase enzymatic activity that facilitates the approach of the virus particle to the immediate cell surface prior to the injection of the viral DNA into the host. The solenoid fold of the TSP carbohydrate binding domains resembles the super-helical structure of an amyloid fibril. Folding and assembly, misfolding and misassembly of the TSP from Salmonella phage P22 have been investigated for more than 30 years. Misassembly of its parallel beta-helix domain leads to amyloid fibrils that may be used as metallization substrates in the generation of nanomaterials. My talk will touch several aspects of our work, from biophysical chemistry to protein evolution and materials science.