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Like other forms of amyloid, aggregated prions form a beta-sheet structure, where individual beta-strands are linked together by hydrogen bonds between their extended peoptide backbones, and hydrophobic interactions between the side chains on either side of the peptide backbone. The beta-strand at each end of the beta-sheet has unpaired hydrogen bonds and ...


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It is thought that infectious prions exist as clusters forming a crystalline structure. When a protein with the same primary structure is encountered but with a different tertiary structure, the normal protein undergoes a conformational change in order to integrate into the cluster. Presumably there are molecular forces involved that induce the ...



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