Abstract
We conducted measurements on unidirectional freezing and circular dichroism for preheated solution and unheated solution of a polypeptide based on winter flounder antifreeze protein. The interface temperature were measured with a thermocouple. The secondary structure of this polypeptide was measured with circular dichroism spectrophotometer. It was found from the circular dichroism spectra that the polypeptide had a β-sheet structure. Although the interface temperature for the unheated solution of the polypeptide did not drop, the interface temperature for the preheated solution showed significant dropped.
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