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Day One Invited Speakers

Professor Ken Ritchie, Purdue Membranes in cells act not only as a structural element to separate compartments within the cell and to separate the cell from its environment, but also as a platform for assembly of complex and critical structures required for exchange of both nutrients and information between the interior and the surroundings. In general, we are interested in understanding the dynamic organization of the proteins and lipids in cellular membranes. While a pure lipid bilayer is a psuedo two dimensional fluid, the membranes surounding cells are much more complex due to their complex mixture of lipids, the addition of embedded protein and the possible presence of a sub-surface scaffolding known as the membrane skeleton

Professor Robijn Bruinsma, UCLA My current work concerns the application of theoretical physics and numerical modeling to molecular biology. Emphasis is on the following areas: -Numerical Simulation of Active Proteins and of Gene Transcription. -Self-Assembly of Viruses -Self-Assembly of DNA and the Physics of Chromatin. -Electrostatics of DNA and electrical transport along DNA. -Adhesion of vesicles and cells.

Professor Tom McLeish, Durham Professor McLeish's research interests include: (i) molecular rheology and processing of entangled polymeric fluids (especially the role of molecular topology); (ii) macromolecular biophysics including protein dynamics, folding and interactions, and biological self-assembly; (iii) issues of theology, ethics and science.

Professor Kevin W. Plaxco, UCSB Our research program is comprised of closely allied applied and basic thrusts. The aim of our applied research is to harness the speed and specificity of biopolymer folding as a signal transduction mechanism in a novel and highly general class of real-time, “real-world” optical and electronic biosensors. In related studies we are exploiting the extraordinary cooperativity of folding for the creation of adaptive, responsive surfaces and materials. The goal of our basic research is the development and testing of a quantitative, first principles theory of the mechanism by which proteins fold. Related theoretical and experimental projects include intensive studies of the structure and dynamics of the unfolded state and the collective dynamics of the native state.