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Direct observation of protein folding, aggregation, and a prion-like conformational conversion
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F. Ding, J.J. LaRocque, and N.V. Dokholyan Direct observation of protein folding, aggregation, and a prion-like conformational conversion J Biol Chem 280 2005 40235 40240 The authors demonstrated the transferability of a force-field developed for a simplified protein model. In addition, they reported the direct observation of the prion-like conformational interconversion of peptides into amyloid-like structures, whereby two peptides that have adopted β-hairpin conformations promote such interconversion of the third peptide. This study suggested a possible generic molecular mechanism for the template-mediated aggregation process, originally proposed by Prusiner to account for prion infectivity.
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(2005)
J Biol Chem
, vol.280
, pp. 40235-40240
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Ding, F.1
Larocque, J.J.2
Dokholyan, N.V.3
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