During long time, lanthanides were thought to be biologically inert. However, the last decade has seen the discovery and development of the field of native lanthanide biochemistry. Lanthanides exhibit a variety of interesting photophysical properties from which many useful applications derive. The development of effective functional lanthanide complexes requires control of their coordination sphere; something proteins manage very effectively through their 3D metal-binding sites. α-Helical coiled coil peptides are miniature scaffolds which can be designed de novo and can retain the favourable properties of larger proteins within a much simplified system. Metal binding sites, including those which bind lanthanides can be engineered into the coiled coil sequence. Here you can see a recently deposited structure determined by X-ray crystallography and depicting how an engineered coiled-coil protein can selectively bind Terbium (III) ions, represented as magenta spheres (PDB code: 7P3H)
#molecularart ... #immolecular ... #lanthanide ... #terbium ... #proteinengineering ... #coiledcoil ... #domain ... #capture ... #coordination ... #Xray ... Rendered with @proteinimaging and polished with @corelphotopaint
#molecularart ... #immolecular ... #lanthanide ... #terbium ... #proteinengineering ... #coiledcoil ... #domain ... #capture ... #coordination ... #Xray ... Rendered with @proteinimaging and polished with @corelphotopaint
