## Abstract Differential scanning calorimetry studies have been carried out on the sequential polypeptide of elastin, (L‐Val^1^–L‐Pro^2^–Gly^3^–L‐Val^4^–Gly^5^)~__n__,~ abrreviated as PPP, and its more hydrophobic analogues (L‐Val^1^–L‐Pro^2^–Gly^3^–L‐Val^4^–Gly^5^)~__n__~, referred to as Leu^1^‐PP
Phase-structure transitions of the elastin polypentapeptide–water system within the framework of composition–temperature studies
✍ Scribed by D. W. Urry; T. L. Trapane; K. U. Prasad
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1985
- Tongue
- English
- Weight
- 637 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The temperature dependence of the composition of coacervate and equilibrium phases is examined for the polypentapeptide of elastin (~-Val~-~-Pro~-Gly~-~-Val~-Gly~)~ in water. This provides for the development of a phase diagram. CD data is presented that provides information on associated polypeptide structure changes that, when added to previous CD, nmr, and dielectric relaxation data a t lower water composition, allow construction of a phase-structure diagram of the polypentapeptide-water system. The molecular-weight dependence of phase change (coacervation) is included. The volumecomposition studies as a function of temperature also provide temperature coefficients of expansion and of composition important in analyzing the mechanism of elasticity.
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