Spectroscopic studies on elastin-like synthetic polypeptides.

A Castiglione-Morelli; A Scopa; A M Tamburro; V Guantieri

doi:10.1016/0141-8130(90)90044-b

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Spectroscopic studies on elastin-like synthetic polypeptides.

A Castiglione-Morelli·A Scopa·A M Tamburro·V Guantieri

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Abstract

Spectroscopic studies on synthetic polypeptides containing the unit-X-G-G (X=V or L) are reported. The sequences, constituting either fragments or model of elastin, were shown to adopt type II beta-turns together with an ensemble of unordered conformations. Furthermore, it was found that the stability of the beta-turns was depending on the nature of the X residue, on the hydration of the chain and, in the case of the sequence G-V-G-G-L, was decreasing by increasing the length of the chain.

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Amino Acid Sequence Circular Dichroism Elastin Magnetic Resonance Spectroscopy Molecular Sequence Data Peptides Protein Conformation Temperature Journal Article

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A Castiglione-Morelli, A Scopa, A M Tamburro, V Guantieri. 1990. Spectroscopic studies on elastin-like synthetic polypeptides.. https://doi.org/10.1016/0141-8130(90)90044-b

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