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Dr Konrad Beck

Dr Konrad Beck

Lecturer in Protein Biophysics, School of Dentistry

School of Dentistry

My main work relates to the structure, folding and assembly of multidomain proteins, especially those of the extracellular matrix.


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


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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Tissue engineering and repair expertise

Structure, folding and assembly of multidomain proteins, specifically those of the extracellular matrix (collagens, laminins, nidogens, tenascins, matrilins); alpha-helical coiled coils; protein sequence/structure relationship.

Circular Dichroism (CD) spectroscopy: An AVIV CD215 with a thermostated cell holder is available. CD spectroscopy can be useful to

a) estimate the secondary structure of proteins
b) determine whether mutations affect the structure, stability or binding interactions
c) determine the thermodynamics of folding of proteins, peptides and DNA
d) determine the kinetics of folding or drug binding.

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 makes it important to elucidate the structural properties of the triple-helix. 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. Some small organic molecules (amino acids and derivatives, carbohydrates, methylamines) seem also to act as effective chemical chaperones. My work wants to further the understanding of the chain association, folding, and interaction of collagenous and -helical coiled coil protein domains, and to investigate the influence of chemical chaperones.

Recent review papers:
P. Rousselle and K. Beck (2013). Laminin 332 processing impacts cellular behavior. Cell Adh. Migr. 7, 122-134.
V. Bauerová-Hlinková, J. Bauer, E. Hostinová, J. Gašperík, K. Beck, Ľ. Borko, A. Faltínová, A. Zahradníková and J. Ševčík (2011). Bioinformatics domain structure prediction and homology modeling of human ryanodine receptor 2. in: Bioinformatics - Trends and Methodologies, M. A. Mahdavi (ed.), chapter 16, pp 325-352. ISBN: 978-953-307-282-1, InTech, DOI: 10.5772/24125.