Investigation of self-assembling hybrid proteins of bacteriophage rak2

Investigation of Self-assembling Hybrid Proteins of Bacteriophage RaK2 DNA, peptides and proteins are tried to be used as building blocks for nanostructures due to their special ablity to self-assemble. Therefore, the main goal of this work was to construct different hybrid proteins which would be fusions of recombinant vB_KleM_RaK2 (RaK2) bacteriophage tail sheath protein truncated 200 amino acid residues at the C-terminal with four different proteins (HpyE – flavin-dependent reductase, 45T3 – esterase, GFP - green fluorescent protein, MBP - maltose-binding protein). The constructions should self-assemble into tube structures and have enzymatic activity. During this work six different hybrid proteins 041del200_GFP, 041del200_HpyE, 041del200_RimI, 041del200_GS_HpyE, 041del200_GS_RimI and 041_MBP were constructed. Among all constructs investigated, 041del200_HpyE, 041del200_RimI, 041del200_GS_HpyE and 041del200_GS_RimI were not enzymatically active, only hybrid protein 041del200_GFP had fluorescent activity. All constructed hybrid proteins self-assembled into tube structures, except 041_MBP