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</script>The birefringence of tropomyosin crystals was measured in the temperature range 5 degrees-35 degrees C. The experimental results are compared with a simple model calculation based on the theory developed by Wiener for the optical properties of colloidal systems. The difference between experimental and theoretical values is less than 15%, which denotes a good agreement given the simplicity of the model. A value of 0.011 was obtained for the intrinsic birefringence of the tropomyosin molecule. The temperature dependence of the crystal birefringence could be accounted for in part by a change of the unit cell parameters; this change was experimentally observed by others in x-ray diffraction experiments.
Birefringence, Crystallography, Protein Conformation, Biophysics, Tropomyosin, Models, Theoretical, Mathematics
Birefringence, Crystallography, Protein Conformation, Biophysics, Tropomyosin, Models, Theoretical, Mathematics
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