Ewch i’r prif gynnwys
Dr Konrad Beck

Dr Konrad Beck

Darlithydd mewn Bioffiseg Proteinau

Ysgol Deintyddiaeth

Qualifications

1990 'venia legendi docendi' in Biophysics ('Habilitation'); thesis work on Correlation of Primary Structure Analysis and Electron Microscopy of Multidomain Proteins, Johannes Kepler University, Department of Physics, Linz, Austria

1984 Ph.D. in Biology; thesis work on translation diffusion and phase separation in lipid monolayers, Max-Planck-Institute for Biophysics, Department of Cell Physiology, Frankfurt am Main, Germany

1981 Diploma in Physics; thesis work on thin film optics and quantitative light microscopy, Johann Wolfgang Goethe University, Frankfurt am Main, Germany

Appointments

2002 - 2004 Research Associate, University of Wales College of Medicine, Dental School, Cardiff, U.K.

spring 2002 Visiting Scientist, Nagoya University, School of Bioagricultural Sciences, Nagoya, Japan; sponsored by the Ministry of Education, Science, Culture and Sports of Japan

1999 - 2001 fellow of the Fondation pour la Recherche Mà dicale, Paris; Institute de Biologie et Chimie des Protà ines, Unità Mixte de Recherche no 5086 du C.N.R.S., Lyon, France

1998 - 1999 Visiting Professor, Nagoya University BioScience Center, Nagoya, Japan; sponsored by the Ministry of Education, Science, Culture and Sports of Japan

1997 - 1998 adjunct Assistant Professor, Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ, U.S.A.

1992 - 1996 Research Associate, Shriners Hospital for Children, Research Unit, Portland, OR, U.S.A.

1990 - 1992 Research Associate and Member of the Faculty of Technics and Sciences, Department of Physics, Johannes Kepler University, Linz, Austria

1988 - 1989 Research Fellow of the German National Science Foundation (DFG), work at the Institute for Biophysics, University of Linz, Austria

1984 - 1988 Research Associate, Department of Biophysical Chemistry, Biocenter, University of Basel, Switzerland

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Research Projects

Current funding: Research into Ageing (2007/08)

Folding and Stability of &lcirc;±-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 &lcirc;±-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 &lcirc;±-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.