NMR structure of the mouse prion protein domain PrP(121-231)

Article Abstract:

The nuclear magnetic resonance structure of the mouse prion protein (PrP) region, composed of the 121st to the 231st amino acids, shows the presence of three alpha-helices and two anti-parallel beta-sheets. A disulfide bond joins the second and third helices. Positive and negative charges are randomly distributed in PrP. Mutations that cause prion diseases occur in the residues present in or around the secondary protein structure. The beta-sheet is probably involved in the conversion of the noninfective protein form to the infective form.

Usage, Proteins, Prions, Prions (Proteins), Protein structure, Nuclear magnetic resonance

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Infectious Alzheimer's disease?

Article Abstract:

The accumulation of organized, self-polymerizing protein aggregates is a hallmark of Alzheimer's disease and infectious prion diseases. The research has shown that amyloids of the amyloid-[beta] (A[beta]) peptide, which is associated with Alzheimer's disease, behaves like an infectious agent when injected into the brain of a mouse model of Alzheimer's disease, generating phenotypes that depend on both the host and the agent.

Science & research, California, Genetic aspects, Alzheimer's disease, Amyloid beta-protein, Prion diseases

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