Description

Amyloid-Forming peptide GNNQQNY is a biological active peptide. (This is a heptapeptide from the N-terminal prion-determining domain of the yeast protein Sup35 that forms amyloid fibrils. The availability of its detailed atomic oligomeric structure makes it a good model for studying the early stage of aggregation. The GNNQQNY dimer forms three stable sheet structures. in-register parallel, off-register parallel, and anti-parallel. The in-register parallel dimer, which is close to the amyloid beta-sheet structure, has few interpeptide hydrogen bonds, making hydrophobic interactions more important and increasing the conformational entropy compared to the anti-parallel sheet.)—Neuroscience-Neurodegeneration–C33H48N12O14——339091-39-3–836.81—-OC(C=C1)=CC=C1C[C@@H](C(O)=O)NC([C@H](CC(N)=O)NC([C@H](CCC(N)=O)NC([C@H](CCC(N)=O)NC([C@H](CC(N)=O)NC([C@H](CC(N)=O)NC(CN)=O)=O)=O)=O)=O)=O–Others–10 mM in DMSO–Amyloid-β—-Neuronal Signaling–Peptides