PrP (127-147) encompasses a prion protein region contributing to conformational conversion and aggregation. Mixed polar and hydrophobic residues promote β-structure formation and intermolecular contacts. Dynamic folding behavior allows examination of early oligomerization events. Researchers use it to dissect sequence determinants of prion stability and misfolding.
CAT No: P10005
1. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
5. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
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