{"paper":{"title":"Dynamic transition from $\\alpha$-helices to $\\beta$-sheets in polypeptide superhelices","license":"http://arxiv.org/licenses/nonexclusive-distrib/1.0/","headline":"","cross_cats":["cond-mat.mtrl-sci","cond-mat.soft","physics.chem-ph"],"primary_cat":"physics.bio-ph","authors_text":"Artem Zhmurov, Kenneth A. Marx, Kirill A. Minin, Prashant K. Purohit, Valeri Barsegov","submitted_at":"2017-03-08T17:22:11Z","abstract_excerpt":"We carried out dynamic force manipulations $in$ $silico$ on a variety of superhelical protein fragments from myosin, chemotaxis receptor, vimentin, fibrin, and phenylalanine zippers that vary in size and topology of their $\\alpha$-helical packing. When stretched along the superhelical axis, all superhelices show elastic, plastic, and inelastic elongation regimes, and undergo a dynamic transition from the $\\alpha$-helices to the $\\beta$-sheets, which marks the onset of plastic deformation. Using Abeyaratne-Knowles formulation of phase transitions, we developed a theory to model mechanical and k"},"claims":{"count":0,"items":[],"snapshot_sha256":"258153158e38e3291e3d48162225fcdb2d5a3ed65a07baac614ab91432fd4f57"},"source":{"id":"1703.02922","kind":"arxiv","version":2},"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"}