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Polypeptide models of elastin: CD and NMR studies on synthetic poly(X-Gly-Gly)

✍ Scribed by Prof. A. M. Tamburro; V. Guantieri; A. Scopa; J. M. Drabble

Publisher: John Wiley and Sons
Year: 1991
Tongue: English
Weight: 502 KB
Volume: 3
Category: Article
ISSN: 0899-0042
DOI: 10.1002/chir.530030417

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✦ Synopsis

Poly(X-Gly-Gly), simple structural models for the hydrophobic, proline-devoid, regions of elastin, have been synthesized and studied by circular dichroism and NMR spectroscopies. The results gave evidence of type I1 p-turns as the only ordered structure present in the polymers. The stability of the turns has been shown to decrease on hydration and to increase in the series Leu < Ala < Val < Ile.

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Sequential polypeptides (L-Arg-X-Gly), were prepared as synthetic models of arginine-rich histones t o study their structure and their stereospecific interactions with DNA. In our previous work the conformational characteristics of poly(L-Arg-L-Ala-Gly), poly(L-Arg-L-Val-Gly), and poly( L-Arg-L-Leu-