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. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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