Dr Konrad Beck
Current funding: Research into Ageing (2007/08)
Folding and Stability of α-Helical Coiled-Coil and Collagenous Proteins
The ability of a polypeptide to fold into its unique, functional tertiary structure depends on its amino acid sequence as well as its environment. Many disease-causing mutations and modifications exert their effects by interference with the proper folding process. The involvement of collagen in connective tissue diseases and other proteins makes it important to elucidate the structural properties of the triple-helix. Understanding the oligomerization state of α-helical coiled coil proteins based on sequence information is still difficult. The influence of the chemical environment on protein folding and stability in general, and especially for fibrous proteins, has only recently attracted some attention. Thus in vivo biosynthesis occurs in a very crowded surroundings, and molecular chaperones help to ensure proper folding and prevent aggregation. Our research is aimed at a better understanding of the chain association, folding, and interaction of collagenous and α-helical coiled coil protein domains, and the importance of cofactors
In Vitro Modulation of Alzheimer's Amyloid Fibril Formation by Small Organic Cofactors
Several neurological diseases appearing late in life (e.g. Alzheimer's) are characterized by a loss of memory and a decline in the ability to perform routine tasks. These disorders are due to the malfunction of different proteins resulting in aggregation (amyloid plaques). Aggregation depends on the proteins and their environment. We try to simulate conditions to regulate the aggregation and study the effect of small molecules. Aggregation and structure are determined by spectroscopic techniques, electron microscopy and X-ray analysis. The results should help in a better understanding of the mechanism of how proteins switch their normal into a disordered state.