Temperature dependence of length of elastin and its polypentapeptide
✍ Scribed by Dan W. Urry; Bryant Haynes; R. Dean Harris
- Book ID
- 117057051
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 341 KB
- Volume
- 141
- Category
- Article
- ISSN
- 0006-291X
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## 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
Molecular dynamics simulations out to 100 ps have been carried out at 300 K in vacuo on the repeating pentapeptide, (VPGVG), of the elastin fiber. The structure employed in the simulation is a p-spiral (helical structure) with 2.7 pentamers per turn and with a 9.45 A rise per turn and 21.6 A rise pe
## Abstract It is suggested that the temperature‐dependent swelling behavior of water‐swollen elastin is due entirely to the interaction of the numerous nonpolar groups in the elastin protein wiht the aqueous swelling solvent (i.e., ahydrophobic interaction). Flory‐Rehner theory for network swellin
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 polypeptid