Dr Konrad Beck

Darlithydd mewn Bioffiseg Proteinau

: beckk@cardiff.ac.uk
: +44 29207 42639

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 MÃ dicale, Paris; Institute de Biologie et Chimie des ProtÃ ines, UnitÃ 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

2001

Goto, A.et al. 2001. A Drosophila haemocyte-specific protein, hemolectin, similar to human von Willebrand factor. Biochemical Journal 359(1), pp. 99-108. (10.1042/0264-6021:3590099)
Beck, K. 2001. Matrilins. In: Kazazian, H. H. J. et al. eds. Wiley Encyclopedia of Molecular Medicine., Vol. 3. New York: Wiley, pp. 2013-2015., (10.1002/0471203076.emm0986)

2000

Beck, K.et al. 2000. Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine. Proceedings of the National Academy of Sciences of the United States of America 97(8), pp. 4273-4278. (10.1073/pnas.070050097)
Yamaguchi, H.et al. 2000. High and low affinity heparin-binding sites in the G domain of the mouse laminin alpha 4 chain. Journal of Biological Chemistry 275(38), pp. 29458-29465. (10.1074/jbc.M003103200)

1999

Ackerman, M. S.et al. 1999. Sequence dependence of the folding of collagen-like peptides: Single amino acids affect the rate of triple-helix nucleation. Journal of Biological Chemistry 274(12), pp. 7668-7673. (10.1074/jbc.274.12.7668)
Tongaonkar, P.et al. 1999. Characterization of a Temperature-Sensitive Mutant of a Ubiquitin-Conjugating Enzyme and Its Use as a Heat-Inducible Degradation Signal. Analytical Biochemistry 272(2), pp. 263-269. (10.1006/abio.1999.4190)
Niimi, T.et al. 1999. A Drosophila gene encoding multiple splice variants of Kazal-type serine protease inhibitor-like proteins with potential destinations of mitochondria, cytosol and the secretory pathway. European Journal of Biochemistry 266(1), pp. 282-292. (10.1046/j.1432-1327.1999.00873.x)

1998

Zeng, B.et al. 1998. Chicken FK506-binding protein, FKBP65, a member of the FKBP family of peptidylprolyl cis-trans isomerases, is only partially inhibited by FK506. Biochemical Journal 330(1), pp. 109-114.
Beck, K. and Brodsky, B. 1998. Supercoiled protein motifs: the collagen triple-helix and the α-helical coiled coil. Journal of Structural Biology 122(1-2), pp. 17-29. (10.1006/jsbi.1998.3965)
Pan, O. H. and Beck, K. 1998. The C-terminal domain of matrilin-2 assembles into a three-stranded alpha-helical coiled coil. Journal of Biological Chemistry 273(23), pp. 14205-14209. (10.1074/jbc.273.23.14205)

1997

Beck, K.et al. 1997. A single amino acid can switch the oligomerization state of the alpha-helical coiled-coil domain of cartilage matrix protein. EMBO Journal 16(13), pp. 3767-3777. (10.1093/emboj/16.13.3767)
Chan, V. C.et al. 1997. Positional preferences of ionizable residues in Gly-X-Y triplets of the collagen triple-helix. Journal of Biological Chemistry 272(50), pp. 31441-31446. (10.1074/jbc.272.50.31441)
Beck, K.et al. 1997. Secondary structure and shape of plasma sex steroid-binding protein - comparison with domain G of laminin results in a structural model of plasma sex steroid-binding protein. European Journal of Biochemistry 247(1), pp. 339-347. (10.1111/j.1432-1033.1997.00339.x)

1996

Beck, K.et al. 1996. Triple helix formation of procollagen type I can occur at the rough endoplasmic reticulum membrane. Journal of Biological Chemistry 271(35), pp. 21566-21573. (10.1074/jbc.271.35.21566)
Beck, K.et al. 1996. The C-terminal domain of cartilage matrix protein assembles into a triple-stranded alpha-helical coiled-coil structure. Journal of Molecular Biology 256(5), pp. 909-923. (10.1006/jmbi.1996.0137)
Nomizu, M.et al. 1996. Mechanism of laminin chain assembly into a triple-stranded coiled-coil structure. Biochemistry 35(9), pp. 2885-2893. (10.1021/bi951555n)

1995

Beck, K. and Gruber, T. 1995. Structure and Assembly of Basement Membrane and Related Extracellular Matrix Proteins. In: Richardson, P. D. and Steiner, M. eds. Principles of Cell Adhesion. Boca Raton: CRC press, pp. 219-252.

1993

Beck, K.et al. 1993. Ionic interactions in the coiled-coil domain of laminin determine the specificity of chain assembly. Journal of Molecular Biology 231(2), pp. 311-323. (10.1006/jmbi.1993.1284)

1992

Kallunki, P.et al. 1992. A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment. Journal of cell biology 119(3), pp. 679-693. (10.1083/jcb.119.3.679)
Beck, K.et al. 1992. Structural motifs of the extracellular matrix proteins laminin and tenascin. In: Taylor, W. R. ed. Patterns in Protein Sequence and Structure. Springer Series in Biophysics Vol. 7. Berlin: Springer Verlag, pp. 229-254.

1991

Chiquet, M.et al. 1991. Isolation of chick tenascin variants and fragments: A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant. European Journal of Biochemistry 199(2), pp. 379-388. (10.1111/j.1432-1033.1991.tb16134.x)
Engel, J.et al. 1991. Assembly of laminin isoforms by triple- and double-stranded coiled-coil structures. Biochemical Society Transactions 19(4), pp. 839-843.
Schmid, V.et al. 1991. The extracellular matrix (mesoglea) of hydrozoan jellyfish and its ability to support cell adhesion and spreading. Hydrobiologia 216-17(1), pp. 3-10. (10.1007/BF00026436)

1990

Beck, K., Hunter, I. and Engel, J. 1990. Structure and function of laminin: anatomy of a multidomain glycoprotein. The FASEB Journal 4(2), pp. 148-160.
Hunter, I.et al. 1990. Evidence for a specific mechanism of laminin assembly. European Journal of Biochemistry 188(2), pp. 205-211. (10.1111/j.1432-1033.1990.tb15391.x)
Beck, K. and Duenk, R. M. 1990. Flexibility of bacteriophage M13: Comparison of hydrodynamic measurements with electron microscopy. Journal of Structural Biology 105(1-3), pp. 22-27. (10.1016/1047-8477(90)90094-S)

1989

Spring, J., Beck, K. and Chiquet-Ehrismann, R. 1989. Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell 59(2), pp. 325-334. (10.1016/0092-8674(89)90294-8)
Beck, K. 1989. Structural model of vinculin: correlation of amino acid sequence with electron-microscopical shape. FEBS Letters 249(1), pp. 1-4. (10.1016/0014-5793(89)80002-X)

1988

Chiquet, M., Masudanakagawa, L. and Beck, K. 1988. Attachment to an endogenous laminin-like protein initiates sprouting by leech neurons. Journal of Cell Biology 107(3), pp. 1189-1198. (10.1083/jcb.107.3.1189)
Chiquet-Ehrismann, R.et al. 1988. Tenascin interferes with fibronectin action. Cell 53(3), pp. 383-390. (10.1016/0092-8674(88)90158-4)
Masuda-Nakagawa, L., Beck, K. and Chiquet, M. 1988. Identification of molecules in leech extracellular matrix that promote neurite outgrowth. Proceedings of the Royal Society of London Series B Containing Papers of a Biological Character Royal Society 235(1280), pp. 247-257. (10.1098/rspb.1988.0074)

1987

McCarthy, R. A., Beck, K. and Burger, M. M. 1987. Laminin is structurally conserved in the sea urchin basal lamina. Embo Journal 6(6), pp. 1587-1593.
Paulsson, M.et al. 1987. Laminin-nidogen complex: Extraction with chelating agents and structural characterization. European Journal of Biochemistry 166(1), pp. 11-19. (10.1111/j.1432-1033.1987.tb13476.x)
Beck, K. 1987. Mechanical concepts of membrane dynamics: Diffusion and phase separation in two dimensions. In: Bereiter-Hahn, J., Anderson, O. R. and Reif, W. eds. Cytomechanics: The Mechanical Basis of Cell Form and Structure. Heidelberg: Springer Verlag, pp. 79-99.

1985

Beck, K. and Peters, R. 1985. Translational diffusion and phase separation in phospholipid monolayers: A fluorescence microphotolysis study. In: Bailey, P. M. and Dale, R. E. eds. Spectroscopy and the dynamics of molecular biological systems. London: Academic Press, pp. 177-196.

1983

Peters, R. and Beck, K. 1983. Translational Diffusion in Phospholipid Monolayers Measured by Fluorescence Microphotolysis. Proceedings of the National Academy of Sciences of the United States of America 80(23), pp. 7183-7187. (10.1073/pnas.80.23.7183)

1981

Beck, K. and Bereiter-Hahn, J. 1981. Evaluation of reflection interference contrast microscope images of living cells. Microscopica Acta 84(2), pp. 153-178.
Bereiter-Hahn, J.et al. 1981. Locomotion of Xenopus epidermis cells in primary culture. Journal of Cell Science 52, pp. 289-311.

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.

Delweddau

No results were found

Dr Konrad Beck

Qualifications

Appointments

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