Secondary structure of [Val. Ala]sCT- an analog of salmon calcitonin (sCT) not containing an N-terminal disultide bridge. was investigated by circular dichroism (CD) and Fourier-transform intrared spectroscopy (FTIR) methods. Both CD and FTIR results show that the main contbrmational structure of [Val Ala’]sCT in aqueous solution is random coil structure. while in trifluorethanol (TFE) it displays a strong α-helical structure. The relationship between the biological activity and the conformational structure of [Val, Ala] sCT is als0 discussed.
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