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The Hypothesis of the Catalytic Action of Nucleic Acid on the Conversion of Prion Protein

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The main hypothesis for prion diseases proposes that the cellular protein (PrPC) can be altered into a misfolded, β-sheet-rich isoform (PrPSc). We describe here that host nucleic acid may catalyze the conversion between PrPC and PrPSc isoforms, by reducing the protein mobility and by making the protein-protein interactions more likely. We summarize the findings, focusing in the biological relevance of the catalytic action of nucleic acid.

Keywords: aggregation; catalysis; nucleic acid; prion; structural conversion

Document Type: Review Article


Affiliations: Departamento de Bioquimica Medica, Centro Nacional de Ressonancia Magnetica Nuclear de Macromoleculas, Instituto de Ciencias Biomedicas, Universidade Federal do Rio de Janeiro, RJ 21941-590, Brazil.

Publication date: April 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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