… “double-hydrophobic” elastin-… hydrophobic domains of native elastin, a protein that provides
elasticity and resilience to connective tissues. In this study, the effects of trifluoroethanol (TFE…

… However, we also demonstrate that the major effect of TFE to promote coacervation in these
elastin-like polypeptides is not due to increased α-helical structure in cross-linking domains …

… on the other can also melt the hydrophobic cores of globular proteins. The … effect of TFE on
a short elastin peptide, GVG(VPGVG) 3 , which forms type II β-turns stabilized by hydrophobic …

… When the temperature effect in trifluoroethanol and the … As discussed in the a-elastin and
tropoelastin studies [8,9], an … , requires that the hydrophobic effect be the predominant force in …

… suggests that hydrophobic interactions are important in the ordered association of a-… for
their ability to interact with elastin in trifluoroethanol. Be 2+ had no apparent effect, while SI + was …

… The effect due to the limited accessibility of water on a short elastin peptide was previously
described in mixed 2,2,2-trifluoroethanol (TFE)/water solutions.61 In support of the …

… ‐hydrophobic elastin‐like triblock polypeptide called GPG, designed after the uneven
distribution of two different hydrophobic domains found in elastin, an … be a potential elastin‐mimetic …

… , short elastin peptides were designed to test the effect of … Of specific interest was the
effects of charge adjacent to the … largest effect was seen below 35% TFE, where hydrophobic …

… -hydrophobic elastin-like polypeptides (ELPs). The hydrogels are obtained with the
double-hydrophobic … Although the kinetics of hydrogel formation is slower for the double-hydrophobic …

… -Gly-Val-Ala-Pro, and hydrophilic domains with many Lys and Ala … hydrophobic domains
of the elastin molecule juxtapose lysine residues involved in crosslinking. Three hydrophobic …