{"paper":{"title":"The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth","license":"http://creativecommons.org/licenses/by/4.0/","headline":"","cross_cats":["physics.bio-ph","q-bio.BM"],"primary_cat":"cond-mat.soft","authors_text":"Alessia Peduzzo, Alexander Hofmann, Alexander K. Buell, Daniel E. Otzen, Erik van Dijk, Georg Groth, Halima Mouhib, Juami Hermine Mariama van Gils, Sanne Abeln","submitted_at":"2019-06-13T12:01:37Z","abstract_excerpt":"Many proteins have the potential to aggregate into amyloid fibrils, which are associated with a wide range of human disorders including Alzheimer's and Parkinson's disease. In contrast to that of folded proteins, the thermodynamic stability of amyloid fibrils is not well understood: specifically the balance between entropic and enthalpic terms, including the chain entropy and the hydrophobic effect, are poorly characterised. Using simulations of a coarse-grained protein model we delineate the enthalpic and entropic contributions dominating amyloid fibril elongation, predicting a characteristic"},"claims":{"count":0,"items":[],"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"source":{"id":"1906.05620","kind":"arxiv","version":1},"verdict":{"id":null,"model_set":{},"created_at":null,"strongest_claim":"","one_line_summary":"","pipeline_version":null,"weakest_assumption":"","pith_extraction_headline":""},"references":{"count":0,"sample":[],"resolved_work":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57","internal_anchors":0},"formal_canon":{"evidence_count":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"author_claims":{"count":0,"strong_count":0,"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"builder_version":"pith-number-builder-2026-05-17-v1"}