Research Department "Cellular Biochemistry" (F.-Ulrich Hartl)
Proteins must fold into well-defined three-dimensional structures in order to become functionally active. This folding process often does not work spontaneously. May proteins require the help of molecular chaperones to fold properly and to avoid clumping together into useless (or even toxic) aggregates. Scientists in the Research Department of “Cellular Biochemistry” headed by F.-Ulrich Hartl aim at elucidating how the chaperones achieve this important task. For example, they have deciphered at great detail the mechanisms by which a subgroup of chaperones, the chaperonins, mediate protein folding. GroEL/GroES, the best known chaperonin, is shaped like a cylinder with a lid, as shown in the image. It encloses a single molecule of unfolded protein in its interior chamber and allows it to fold in isolation, thereby avoiding aggregation with other unfolded proteins. The research conducted by Ulrich Hartl and his team could make a significant contribution to the development of new therapeutic strategies for diseases like Parkinson’s or Alzheimer’s, which are caused by the deposition of protein aggregates in the brain.