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

S. Abdel Rahman, M. Elsafty and A. Hattaba

Faculty of Science, Zagazig University, Zagazig, Egypt.

ABSTRACT:

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.

KEYWORDS:

Dichroism; Peptides

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Copy the following to cite this article: Rahman S. A, Elsafty M, Hattaba A. A Circular Dichroism and Infrared Study of β-Turn Formation in Repeat Peptides of Elastin. Orient J Chem 1987;3(1).

Copy the following to cite this URL: Rahman S. A, Elsafty M, Hattaba A. A Circular Dichroism and Infrared Study of β-Turn Formation in Repeat Peptides of Elastin. Orient J Chem 1987;3(1). Available from: http://www.orientjchem.org/?p=42192