Structural characterization of the two T and R conformers of Carcinus aestuarii hemocyanin trapped in sol-gel matrix
This proposal is aimed to the structural characterization of hemocyanins, the oxygen transport proteins of mollusks and arthropods, in order to describe the conformational features that define their affinity for oxygen. Under anaerobic condition the protein exists as T-oxy (tense) state in the deoxygenated form, while under oxygen saturation as R-deoxy (relaxed) state. Neither T-oxy nor R-deoxy can be isolated in solution. Our experimental strategy is based on embedding R and T conformations within the pores of a sol-gel matrix where the reduced mobility of water strongly decreases the rate of the conformational shift that occurs during the oxygen saturation process. In previous SANS measurements within a BAG section (BAG-8-27) we have checked the adequacy of the experiment-targeted sample holders, the gel preparation and the optimum matching contrast conditions between solvent and sol-gel matrix. occurring at 72 mol % D2O. SANS data will be analyzed using a newly developed method that will allow the determination of the quaternary structure differences between the R and the T state.
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SPINOZZI Francesco; BELTRAMINI Mariano; MARIANI Paolo; MINUTE Fabrizio; Ortore M.G. and PORCAR Lionel. (2012). Structural characterization of the two T and R conformers of Carcinus aestuarii hemocyanin trapped in sol-gel matrix. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-755
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