A Circular Dichroism and Infrared Study of β-Turn Formation in Repeat Peptides of Elastin

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The conformation properties of few synthesized Elast in-like peptides were examined in solution using circular dichrotsm at different temperatures < 30°C, 30°C and 70°C ) and in solid state by IR at room temperature. The studies shows that the β-turn is a significant conformational feature for peptides under investigation in solution at 30°C and 50°C. but at 70°C the tetra, hexa and deca peptides shows the CD feature charac teres tic of the p-structure while the dodeca peptide spectral pattern shows the presence of β-turn which indecates the stability of β-turn at this chain length.

Dichroism; Peptides