Amyloid-Forming peptide GNNQQNY [339091-39-3]

Referencia NB-64-86374-50mg

embalaje : 50mg

Marca : Neo Biotech

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Teléfono : +1 850 650 7790

Amyloid-Forming peptide GNNQQNY

Catalog No. T83122 Copy Product Info
Amyloid-Forming peptide GNNQQNY, a biologically active heptapeptide derived from the N-terminal prion-determining domain of yeast Sup35, is instrumental in amyloid fibril formation. Its atomic oligomeric structure has been detailed, serving as an excellent model for investigating early-stage aggregation. The peptide can form three stable β-sheet structures: in-register parallel, off-register parallel, and anti-parallel. Notably, the in-register parallel dimer aligns closely with amyloid β-sheet architecture, relying on fewer interpeptide hydrogen bonds and emphasizing hydrophobic interactions, which enhances conformational entropy relative to the anti-parallel arrangement.

Amyloid-Forming peptide GNNQQNY

Copy Product Info

Amyloid-Forming peptide GNNQQNY, a biologically active heptapeptide derived from the N-terminal prion-determining domain of yeast Sup35, is instrumental in amyloid fibril formation. Its atomic oligomeric structure has been detailed, serving as an excellent model for investigating early-stage aggregation. The peptide can form three stable β-sheet structures: in-register parallel, off-register parallel, and anti-parallel. Notably, the in-register parallel dimer aligns closely with amyloid β-sheet architecture, relying on fewer interpeptide hydrogen bonds and emphasizing hydrophobic interactions, which enhances conformational entropy relative to the anti-parallel arrangement.

Amyloid-Forming peptide GNNQQNY
Cas No. 339091-39-3

Product Introduction

Bioactivity
Description
Amyloid-Forming peptide GNNQQNY, a biologically active heptapeptide derived from the N-terminal prion-determining domain of yeast Sup35, is instrumental in amyloid fibril formation. Its atomic oligomeric structure has been detailed, serving as an excellent model for investigating early-stage aggregation. The peptide can form three stable β-sheet structures: in-register parallel, off-register parallel, and anti-parallel. Notably, the in-register parallel dimer aligns closely with amyloid β-sheet architecture, relying on fewer interpeptide hydrogen bonds and emphasizing hydrophobic interactions, which enhances conformational entropy relative to the anti-parallel arrangement.
Chemical Properties
Molecular Weight836.81
FormulaC33H48N12O14
Cas No.339091-39-3
Smiles[C@H](C(N[C@H](C(N[C@@H](CC1=CC=C(O)C=C1)C(O)=O)=O)CC(N)=O)=O)(NC([C@@H](NC([C@@H](NC([C@@H](NC(CN)=O)CC(N)=O)=O)CC(N)=O)=O)CCC(N)=O)=O)CCC(N)=O
SequenceGly-Asn-Asn-Gln-Gln-Asn-Tyr
Sequence ShortGNNQQNY
Storage & Solubility Information
StoragePowder: -20°C for 3 years | In solvent: -80°C for 1 year Shipping with blue ice/Shipping at ambient temperature.