Abstract
The aggregates of the full-length human recombinant prion protein (PrP) (23-231) on model membranes were investigated by combining the atomic force microscopy (AFM) measurements and theoretical calculations at pH 5.0, showing the great effect of PrP concentration on its supramolecular assemblies on the lipid bilayer.
MeSH terms
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Cell Membrane / chemistry
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Cell Membrane / metabolism*
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Humans
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Hydrogen-Ion Concentration
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Lipid Bilayers / chemistry
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Lipid Bilayers / metabolism
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Microscopy, Atomic Force
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Molecular Docking Simulation
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Prion Proteins / chemistry*
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Prion Proteins / metabolism
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Protein Aggregates*
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Protein Multimerization
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Protein Structure, Quaternary
Substances
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Lipid Bilayers
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Prion Proteins
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Protein Aggregates