The CBP symposium is a truly unique student run meeting and for the past 4 years we have brought together a wonderfully diverse panel of international scientists, all innovators and leaders at the cutting edge of their respective fields. In continuing with this tradition, this years' speakers are no exception to this level of excellence. Our organizing committee is extremely enthusiastic to present the following speakers for CBP 2006:

University of Pennsylvania, USA William Degrado
Dr. DeGrado's primary research interest is in the de novo design of proteins, in which one attempts to design proteins from first principles. This approach critically tests the understanding of protein folding and function, while also laying the groundwork for the design of proteins with properties not precedented in nature. The de novo design of proteins has proven to be a useful approach for understanding the features in a protein sequence that cause them to fold into their unique three-dimensional structures. In addition, the DeGrado lab has recently been able to prepare a variety of functionally interesting proteins that bind redox-active cofactors, DNA, and transition metals.

Jay Groves UC Berkeley, USA
The basic problem addressed is the collective interaction between populations of receptors and ligands in two apposed fluid membranes. We wish to understand how the binding kinetics, lateral mobility of the membrane proteins, membrane bending effects etc. influence molecular organization and recognition. Our approach is aimed toward elucidating how these physico-chemical parameters determine the formation of spatio-temporal patterns at cell signaling junctions. A three-pronged investigative platform combining novel membrane experiments in reconstituted lipid membranes and cell biology with theoretical calculations and computer simulations has been formulated to meet our goals.

Ruprecht-Karls-Universität, Germany Michael Grunze
The objective of the project is to develop methods for the coating of implants with poly([bistrifluorethoxy]phosphazen) and to investigate them und in-vitro und in-vivo. Surface analytical tools such as XPS and AFM are used to characterize the coatings. We also investigate how phosphazen coatings prevent thrombus formation. For this we use immunological methods (ELISA) to mesure the protein adsorption from blood plasma on phosphazen and reference samples. This project is done in collaboration with Heidelberg and external groups as well as industry partners.

Stuart Kauffman University of Calgary, Canada
Stuart Kauffman is a biologist who specializes in the theory of complex systems in biology, including the dynamics of genetic networks, molecular evolution in rugged fitness landscapes, and the origin of life. He has taken an interdisciplinary approach, using ideas from statistical physics and computer science. He was one of the founder members of the Santa Fe institute, a centre for interdisciplinary research in complex systems, and recently founded the Bios Group LP. He has held academic appointments at the University of Chicago, University of Pennsylvania and University of New Mexico.

Waseda University, Japan Kazuhiko Kinosita
In our lab, optical microscopes are the only tool of observation. Although spatial resolution is not as high as with electron microscopes, there is the merit that one can continuously observe, and record, a single molecule performing its function. Molecular machines perform well even when they carry a tag that is hundreds of times as large as their own body. Such tags reveal details of the molecular performances under an ordinary microscope. Small tags such as a single fluorophores can be attached at a desired position in the machine, and it will report on the movement of that particular part. In addition to the observation using huge and small tags, we can manipulate individual molecules with optical and magnetic tweezers. The term 'Single-Molecule Physiology' best describes our endeavors.

Anthony Pawson University of Toronto, Canada
Our focus is on studying the mechanisms that underlie intracellular signal transduction. Modular protein domains that mediate protein-protein interactions are critical elements of this process. These modules are typified by the phosphotyrosine binding Src homology 2 (SH2). Since the discovery of SH2 domains, the number of different modules has grown into the dozens, many of which we continue to investigate. Work on the molecular dissection and functional significance of protein-protein interactions, in signal transduction, is a primary focus of the lab. In addition to this, we are also actively working on the molecular signals involved in axon guidance; wiring the cell through protein interactions especially Eph receptors and ephrins.

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