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 β-turns together with an ensemble of unordered conformations. Furthermore, it was found that the stability of the β-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. © 1990.
Spectroscopic studies on elastin-like synthetic polypeptides
CASTIGLIONE MORELLI, Maria Antonietta;SCOPA, Antonio;TAMBURRO, Antonio Mario;
1990-01-01
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 β-turns together with an ensemble of unordered conformations. Furthermore, it was found that the stability of the β-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. © 1990.File in questo prodotto:
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