title: Rational stabilization of helix 2 of the prion protein prevents its misfolding and oligomerization.
abstract: Designed stabilization of helix 2 of the mouse prion protein is shown to lead to an increase in global stability of the protein. Studies of hydrogen exchange coupled to mass spectrometry confirm that the increase in stability is confined primarily to helix 2, and that it accounts for the global stabilization of the protein. Importantly, such localized stabilization of the protein can completely inhibit its ability to form oligomers and slows down amyloid fibril formation.
authors.affiliation: National Centre for Biological Sciences, Tata Institute of Fundamental Research , Bengaluru 560065, India.
authors.forename: Jogender
authors.initials: J
authors.lastname: Singh
authors.forename: Harish
authors.initials: H
authors.lastname: Kumar
authors.forename: Ambadi T
authors.initials: AT
authors.lastname: Sabareesan
authors.forename: Jayant B
authors.initials: JB
authors.lastname: Udgaonkar
mesh_terms: D000818:Animals; D013058:Mass Spectrometry; D051379:Mice; D011328:Prions / Q000138:chemical synthesis / Q000737:chemistry*; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D011328:Prions