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| Scott Feller, Wabash College |
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Scott Feller was born in Portland, Oregon (U.S.A) in 1967. He earned undergraduate degrees in chemistry and mathematics at Willamette University, a liberal arts college in Oregon. In 1993, he received his PhD from the University of California, Davis where he worked with Donald McQuarrie on the application of statistical mechanical theories of liquids to the structure of the electrical double layer. His postdoctoral training, with Richard Pastor at the Center for Biologics Evaluation and Research on the NIH campus, was in the area of molecular dynamics computer simulations of lipid bilayer membranes.
The development of new simulation techniques and their application to problems in membrane biophysics are the focus of the research program he continues today at Wabash College, a liberal arts college in central Indiana, where he is currently Associate Professor of Chemistry.
The use of MD simulation to interpret experimental data is the common theme among the current projects being pursued in Professor Feller's laboratory. These include the analysis of simulation trajectories to extract quantities which aid in the refinement of x-ray diffraction of fluid bilayers, and the interpretation of NMR relaxation in terms of contributions from various molecular motions. Support for this work comes from the National Science Foundation and the Dreyfus Foundation.
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Understanding the Unique Properties of Polyunsaturated Lipids
Scott Feller, Wabash College
The structure and dynamics of polyunsaturated lipids, specifically those containing docosahexaenoic and docosapentanoic acid, will be described and compared with saturated and mono-unsaturated lipids. Comparison will be made between the simulation results and experimental measurements utilizing NMR and x-ray diffraction. Both simulation and experiment suggest the polyunsaturated fatty acid chains possess an extreme flexibility. The role of the torsional energy profile for rotation about single bonds between vinyl groups will be emphasized as the key factor in these observations. A mechanism by which this flexibility allows unique interactions with integral membrane proteins will be demonstrated.
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