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Abstract

Silk fibroin films in the random-coil and β-form conformations were immersed in water at temperatures from 2 to 130°C, and conformational changes were followed by x-ray diffraction, infrared spectroscopy and differential scanning calorimetry. On treatment with water below 60°C, the random-coil conformation is converted to the α form and above 70°C to mixtures of the α and β conformations. The β-form content increases as the immersion temperature is raised. The β form is not affected by immersion in water in the temperature range studied.