Dr Konrad Beck
Darlithydd mewn Bioffiseg Proteinau
- Email:
- beckk@cardiff.ac.uk
- Telephone:
- +44 29207 42639
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, SwitzerlandQualifications
Appointments
2019
- Da'as, S. I.et al. 2019. Arrhythmogenic calmodulin E105A mutation alters cardiac RyR2 regulation leading to cardiac dysfunction in zebrafish. Annals of the New York Academy of Sciences 1448(1), pp. 19-29. (10.1111/nyas.14033)
- Šebová, R.et al. 2019. Residue mutations in murine herpesvirus 68 immunomodulatory protein M3 reveal specific modulation of chemokine binding. Frontiers in Cellular and Infection Microbiology 9, pp. -., article number: 210. (10.3389/fcimb.2019.00210)
2018
- Jack, A.et al. 2018. Alginate Oligosaccharide-Induced Modification of the lasI-lasR and rhlI-rhlR Quorum Sensing Systems in Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 62(5), article number: e02318-17. (10.1128/AAC.02318-17)
- Bovay, A.et al. 2018. T cell Receptor Alpha Variable 12-2 bias in the immunodominant response to Yellow fever virus. European Journal of Immunology 48(2), pp. 258-272. (10.1002/eji.201747082)
2017
- Cole, D.et al. 2017. Dual molecular mechanisms govern escape at immunodominant HLA A2-restricted HIV epitope. Frontiers in Immunology 8, article number: 1503. (10.3389/fimmu.2017.01503)
- Pritchard, M.et al. 2017. A low molecular weight alginate oligosaccharide disrupts pseudomonal microcolony formation and enhances antibiotic effectiveness. Antimicrobial Agents and Chemotherapy 61(9), article number: e00762-17. (10.1128/AAC.00762-17)
- Fuller, A.et al. 2017. Thermal stability of heterotrimeric pMHC proteins as determined by circular dichroism spectroscopy. Bio-Protocol 7(13), article number: e2366. (10.21769/BioProtoc.2366)
- Pritchard, M. F.et al. 2017. The antimicrobial effects of the alginate oligomer OligoG CF-5/20 are independent of direct bacterial cell membrane disruption. Scientific Reports 7, article number: 44731. (10.1038/srep44731)
- Nomikos, M.et al. 2017. Male infertility-linked point mutation reveals a vital binding role for the C2 domain of sperm PLCζ. Biochemical Journal 474(6), pp. 1003-1016. (10.1042/BCJ20161057)
- Cole, D.et al. 2017. Structural mechanism underpinning cross-reactivity of a CD8+ T-cell clone that recognises a peptide derived from human telomerase reverse transcriptase. Journal of Biological Chemistry 292(3), pp. 802-813. (10.1074/jbc.M116.741603)
2016
- Nomikos, M.et al. 2016. Mutations in PLCd1 associated with hereditary leukonychia display divergent PIP2 hydrolytic function. FEBS Journal 283(24), pp. 4502-4514. (10.1111/febs.13939)
- Ulaeto, D. O.et al. 2016. Destabilization of α-helical structure in solution improves bactericidal activity of antimicrobial peptides: Opposing effects on bacterial and viral targets. Antimicrobial Agents and Chemotherapy, article number: AAC.02146-15. (10.1128/AAC.02146-15)
- Jones, K.et al. 2016. The impact of HLA-class I and EBV-latency-II antigen-specific CD8+T-cells on the pathogenesis of EBV+ Hodgkin Lymphoma. Clinical and Experimental Immunology 183(2), pp. 206-220. (10.1111/cei.12716)
- Roberts, J.et al. 2016. In vitro evaluation of the interaction of dextrin-colistin conjugates with bacterial lipopolysaccharide. Journal of Medicinal Chemistry 59(2), pp. 647-654. (10.1021/acs.jmedchem.5b01521)
2015
- Vassilakopoulou, V.et al. 2015. Distinctive malfunctions of calmodulin mutations associated with heart RyR2-mediated arrhythmic disease. Biochimica et Biophysica Acta (BBA) - General Subjects 1850(11), pp. 2168-2176. (10.1016/j.bbagen.2015.07.001)
- Motozono, C.et al. 2015. Distortion of the major histocompatibility complex class I binding groove to accommodate an insulin-derived 10-Mer peptide. Journal of Biological Chemistry 290(31), pp. 18924-18933. (10.1074/jbc.M114.622522)
- Knight, R. R.et al. 2015. A distinct immunogenic region of glutamic acid decarboxylase 65 is naturally processed and presented by human islet cells to cytotoxic CD8 T cells. Clinical and Experimental Immunology 179(1), pp. 100-107. (10.1111/cei.12436)
- Kløverpris, H. N.et al. 2015. A molecular switch in immunodominant HIV-1-specific CD8 T-cell epitopes shapes differential HLA-restricted escape. Retrovirology 12(1), article number: 20. (10.1186/s12977-015-0149-5)
2014
- Nomikos, M.et al. 2014. Altered RyR2 regulation by the calmodulin F90L mutation associated with idiopathic ventricular fibrillation and early sudden cardiac death. Febs Letters 588(17), pp. 2898-2902. (10.1016/j.febslet.2014.07.007)
- Borko, L.et al. 2014. A regulatory component of the human ryanodine receptor 2 N-terminus. Biophysical Journal 106(2), pp. 107A-107A. (10.1016/j.bpj.2013.11.661)
- Borko, L.et al. 2014. Structural insights into the human RyR2 N-terminal region involved in cardiac arrhythmias. Acta Crystallographica Section D: Biological Crystallography 70(11), pp. 2897-2912. (10.1107/S1399004714020343)
2013
- Blayney, L. M.et al. 2013. ATP interacts with the CPVT mutation-associated central domain of the cardiac ryanodine receptor. Biochimica et Biophysica Acta (BBA) - General Subjects 1830(10), pp. 4426-4432. (10.1016/j.bbagen.2013.05.038)
- Thomas, H.et al. 2013. Transglutaminase 6: A protein associated with central nervous system development and motor function. Amino Acids 44(1), pp. 161-177. (10.1007/s00726-011-1091-z)
- Rousselle, P. and Beck, K. 2013. Laminin 332 processing impacts cellular behavior. Cell Adhesion and Migration 7(1), pp. 122-134. (10.4161/cam.23132)
2012
- Morris, C. J.et al. 2012. Pegylation of antimicrobial peptides maintains the active peptide conformation, model membrane interactions, and antimicrobial activity while improving lung tissue biocompatibility following airway delivery. Antimicrobial Agents and Chemotherapy 56(6), pp. 3298-3308. (10.1128/AAC.06335-11)
- Carulli, S.et al. 2012. Cell surface proteoglycans syndecan-1 and -4 bind overlapping but distinct sites in laminin α3 LG45 protein domain.. The Journal of Biological Chemistry 287(15), pp. 12204-12216. (10.1074/jbc.M111.300061)
2011
- Deacon, S. P. E.et al. 2011. Polymer coiled-coil conjugates: potential for development as a new class of therapeutic "molecular switch". Biomacromolecules 12(1), pp. 19-27. (10.1021/bm100843e)
- Bauerová-Hlinková, V.et al. 2011. Bioinformatics Domain Structure Prediction and Homology Modeling of Human Ryanodine Receptor 2. In: Mahmood, A. M. ed. Bioinformatics – Trends and Methodologies.. Rijeka: InTech, pp. 325-352.
2010
- Bauerová-Hlinková, V.et al. 2010. Bioinformatic mapping and production of recombinant N-terminal domains of human cardiac ryanodine receptor 2. Protein Expression and Purification 71(1), pp. 33-41. (10.1016/j.pep.2009.12.014)
2004
- Yamashita, H., Beck, K. and Kitagawa, Y. 2004. Heparin binds to the laminin a4 chain LG4 domain at a site different from that found for other laminins. Journal of Molecular Biology 335(5), pp. 1145-1149. (10.1016/j.jmb.2003.11.047)
2003
- Utani, A.et al. 2003. Laminin a3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling. Journal of Biological Chemistry 278(36), pp. 34483-34490. (10.1074/jbc.M304827200)
- Matsushima, Y.et al. 2003. Functional domains of chicken mitochondrial transcription factor A for the maintenance of mitochondrial DNA copy number in lymphoma cell line DT40. Journal of Biological Chemistry 278(33), pp. 31149-31158. (10.1074/jbc.M303842200)
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.
Current funding: Research into Ageing (2007/08) Folding and Stability of &lcirc;±-Helical Coiled-Coil and Collagenous Proteins In Vitro Modulation of Alzheimer's Amyloid Fibril Formation by Small Organic CofactorsResearch Projects
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
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.