Spectroscopic studies on elastin-like synthetic polypeptides.
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.
Castiglione-Morelli
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A
Department of Chemistry, Università della Basilicata, Potenza, Italy.
Scopa
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A
Tamburro
A M
AM
Guantieri
V
V
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature
D010455:Peptides; D004549:Elastin