CBC MRes Conference

The CBC MRes Conference will include keynote speeches from Professor Per Hammarstrom and Professor David Klenerman as well as breakout sessions and workshops.

For more information and to register to attend the conference please email Dr Wing-Chau Tung, cbcadmin@imperial.ac.uk or call on 020 7594 5880.

You can also follow this link to view the full agenda for the conference.

Keynote speakers

Professor Per Hammarstrom, Professor of Protein Chemistry, Linkoping University, Sweden will present “Characterization of Pathogenic Amyloidogenic Proteins”.

Abstract: A variety of diseases (Alzheimer´s Disease, Prion diseases and Systemic Amyloidoses) are associated with amyloid deposition. Amyloid deposits are composed of aggregated misfolded protein molecules arranged in a fibrillar morphology. Irrespective of the protein sequence and the native protein fold, the formed amyloid fibrils display remarkably similar structures stabilized by cross-beta-sheet structure of the individual proteins that are aligned perpendicular to the fiber axis. Also common oligomeric intermediates often appear which display a spherical or curvilinear appearance 5-50 nm in diameter. Assemblies of misfolded proteins are transient and conformationally heterogeneous. Also the likely dynamic interplay between oligomers and fibrils is not at all understood. In the laboratory we are searching for common intermediates, oligomers and fibrillar conformations through studies of several proteins associated with amyloid disease. New methods and molecular probes to investigate these species are of interest to widen our understanding of the amyloid diseases. Data collected on the human prion protein, amyloid beta, and transthyretin will be presented entailing protein misfolding studies of these proteins both in vitro and in vivo. The discussions will include novel fluorescent molecular probes, complex protein aggregation pathways and insights from transgenic animal models (Drosophila Melanogaster and mice) of the associated diseases (prionosis, Alzheimer´s and transthyretin amyloid diseases).

Biography: Per Hammarstrom, received his PhD in 2000 at Linkoping University (LiU) and spent two years as a post doctoral fellow at The Scripps Research Institute, in La Jolla, USA. His early research was centered on the role of protein folding intermediates in the protein folding process, and the mechanistic function of molecular chaperones during productive folding. Following his post doctoral years Hammarstrom’s research has shifted towards investigation of protein misfolding and its key role in a wide variety of diseases often called amyloid diseases. His research is focused on protein misfolding, amyloid formation and disease on the molecular level. Hammarstrom has been granted several young investigator awards and is currently a Swedish Royal Academy of Sciences Research Fellow.

Professor David Klenerman,University of Cambridge will present “Studying single molecules on living cells”.

Abstract: One major challenge in biology is to understand how the individual molecules and complexes of the cell are organised and interact to form a functional living cell. To address this problem new sensitive biophysical tools are needed that are capable of studying single molecules in complexes both in the test-tube and on or in living cells.  

To determine the oligomerisation state of proteins we have used two colour single molecule coincidence detection based on the excitation of two distinct fluorophore labels on proteins with two lasers focussed to the same spot. This method requires no prior knowledge of the structure of any complex formed or control of fluorophore position on the molecule. We show that this method can be used to characterise the protein oligomers formed during protein misfolding, ultimately resulting in amyloid fibril formation, and can distinguish between protein monomers and dimers on the cell surface.

Working together with Professor Yuri Korchev at Imperial College, we have developed a method for functional nanoscale mapping of the cell surface that is based on a scanned nanopipette. This allows high resolution, non-contact imaging of the soft and responsive cell surface using the ion current that flows between an electrode in the nanopipette and bath for distance feedback control. Recently we have made a major advance in the resolution of the topographic images, by scanning with fine quartz pipettes, so we can directly visualise protein complexes on the surface of live cells. The pipette can also be use to perform local nanoscale assays on the cell surface so as  to perform single channel recording or apply pressure to probe the mechanical properties. We have also combined high resolution topographic imaging with simultaneous recording of the fluorescence from the cell surface. In addition the pipette can be used for controlled voltage driven delivery and deposition of biomolecules down to the single molecule level and this is being used to probe the structure of the cell membrane using single molecule fluorescence tracking.

Biography: David Klenerman did his PhD under the supervision of Professor I.W.M. Smith FRS in the Department of Chemistry at Cambridge University on infra-red chemiluminescence. He was then a Fulbright Scholar at Stanford University, California doing post-doctoral research with Professor Richard. N. Zare on high overtone chemistry. He then came back to the UK and worked for seven years for BP Research in their Laser Spectroscopy Group before returning to Cambridge University, where he is currently a Professor in Biophysical Chemistry in the Department of Chemistry. His research interests are the development and application of novel biophysical methods to biological and biomedical problems. This includes single molecule fluorescence spectroscopy of individual biomolecules, scanning ion conductance microscopy imaging of living cells and bionanotechnology. He is the author of over 100 papers and 10 patents. He also co-founded Solexa, a high speed DNA sequencing company.