Untitled

Copper in the silk formation process of Bombyx mori silkworm

“…Thus fairly dilute solutions of CuSO 4 can induce the conformation transition in aqueous solutions of silk fibroin from random coil/helical conformation to β‐sheet. This is of considerable interest in that Cu(II) is known to induce the formation of β‐sheet structure in other proteins [35,36]. Of these the prion protein (PrP) is most instructive.…”

Protein Design: Toward Functional Metalloenzymes

“…764,765 Specifically, at pH 5.8, 6.4, and 6.7, betabellin-15D only folds into β -sheets in the presence of Cu(II), signified by a substantial increase in the absolute value of molar ellipticity at 218 nm in the CD spectrum, which was not observed in its apo-protein form. 765 …”

Molecular mimicry of conformationally diverse β-sheets by using α/β-peptide foldamers

“…[18][19][20][21][22][23][24] Another design strategy resulted in higher ordered -sandwich structures with high propensity to aggregation. [97][98][99][100] These designs highlighted the importance of the turn segment as well as the residue composition and the stabilizing interstrand interactions and hydrophobic forces ( Figure 4). These rules that have been established during the de novo design of minimal -sheet model systems and the higher ordered, hydrophobically stabilized -sheets may help us to improve the design strategies and extend to -peptidic systems.…”