EPR Spectrometer Upgrade for Structural Biophysics Core Laboratory

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9970177SummaryFour major and five minor users at the University of Minnesota are acquiring an EPRinstrumentation upgrade to study the dynamics, structure, and function of proteins involved in muscle contraction, membrane calcium transport, photosynthesis, lipid binding and transport, and protein folding. The investigators are studying biological function and mechanism through mutagenesis, protein design, physiology, and enzyme kinetics, as well as a variety of structural techniques, using the shared facilities of a recently established Structural Biophysics Core Laboratory (SBCL). The new instrument has capabilities that will (1) allow experiments on small and precious samples, such as mutant proteins, single muscle fibers, and single protein crystals, and the capability for programmable data-acquisition for time-resolved EPR experiments, (2) include specialized resonators for small oriented samples and for time-resolved photochemical EPR experiments, and (3) has a second higher spectrometer frequency, to increase sensitivity and resolution and decrease ambiguity of data analysis. The structure and dynamics of muscle structural proteins will be detected by EPR simultaneously with muscle mechanics and correlated with the aging process. Transient and multi-frequency EPR will be used to probe the kinetics of turnover of the catalytic site of photosystem II, the photosynthetic water-oxidizing complex. The dynamic interaction between lipid binding proteins and bound lipids will be probed by EPR in solution and single protein crystals and coordinated with x-ray crystallography.