Revisiting the Potential Functionality of the MagR Protein

Recent findings have sparked great interest in the putative magnetic receptor protein MagR. However, vivo experiments revealed no moment of MagR at room temperature. Nevertheless, interaction and fusion proteins with silica-coated magnetite beads proven useful for purification. In this study, we recombinantly produced two different Escherichia coli BL21(DE3) to (1) expand earlier purification studies, (2) test if can magnetize whole E. cells once it is expressed a high cytosolic, soluble titer, (3) investigate MagR-expressing cells’ properties low temperatures. Our results show that induces measurable, permanent temperatures, indicating usability cell magnetization. Furthermore, limited bead-based purification, thus closing current knowledge gap between theoretical considerations empirical data on protein.