(22f) [Invited Talk] Dissecting Thermodynamic Complexities in Lanmodulin Proteins

Lanmodulins – a family of small proteins that undergo large conformational changes in response to binding lanthanides and other rare earth elements – are the first native, reversible, and selective biological chelators for rare earths to be described. The presence of four metal-binding sites in these proteins, as well as the recent observation of a lanmodulin that also dimerizes, presents thermodynamic complications – yet also opportunities – in exploiting these proteins for separation of rare earths. In this talk, I will focus on dissection of order of metal binding, cooperativity, and dimerization effects in lanmodulin proteins. I will relate these properties to the ability to use, and improve, these systems for separations of rare earths.