Inside Back Cover: The Most Stable Protein–Ligand Complex: Applications for One‐Step Affinity Purification and Identification of Protein Assemblies (Angew. Chem. Int. Ed. 18/2012)
Christoph Giese, Franziska Zosel, Chasper Puorger, Rudi Glockshuber · Angewandte Chemie International Edition · 2012
The thermodynamically most stable protein–ligand complex known to date is formed by sections of protein subunits derived from type 1 pili of E. coli. R. Glockshuber and co-workers have developed a new method based on this noncovalent interaction for the single-step affinity purification of protein assemblies from E. coli cell extracts. They describe their insights and the new application in their Communication on page 4474 ff.