It was the key objective of the joint research effort LMU2 (sponsored by ForPrion) to clarify the influence of copper binding on the structure of human PrPC, particularly when bound to a membrane, because the structure of this protein is only known at conditions (slightly acidic
aqueous solution), at which Cu2+ does not bind to PrPC. As is revealed by the attached reportsof the four partners within LMU2, for this purpose a multitude of PrP peptides including the full length protein were recombinantly produced in bacteria (shorter PrP peptides were also synthesized), the influence of Cu2+ binding was measured by many different biophysical methods (NMR, EPR, ENDOR, XAS, ...) using various solvent environments, and the associated molecular structures were determined by simulation-based computational procedures, which were particularly designed for this purpose. In addition, various new methods were investigated and establisched, e.,g. for attaching a lipd anchor to recombinantly produced PrP or to enable more efficient simulations of proteins in solution. For a representation of the multitude of general insights and particular results gained by the project partners during the five year grant period, we refer to the attached summaries and reports of the four project partners.
<P> For more information, please visit the <a href="http://www.bayfor.org/en/portfolio/research-cooperations/world-of-livin…; target="_blank">FORPRION Research Program</a>.