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The fluctuating secondary structure of this intrinsically disordered protein is modelled by dynamic variations of the shape and interaction characteristics of the patchy particles, ranging from spherical with weak isotropic attractions for the disordered state to spherocylindrical with strong directional interactions for a \u03b2-sheet. Flexible linkers between the particles enable sampling of the tertiary structure. This novel model is applied here to study the growth of an amyloid fibril, by calculating the free energy profile of a protein attaching to the end of a fibril. The simulation results suggest that the attaching protein readily becomes trapped in a mis-folded state, thereby inhibiting further growth of the fibril until the protein has readjusted to conform to the fibril structure, in line with experimental findings and previous simulations on small fragments of other proteins.<\/jats:p>","DOI":"10.1063\/1.4978297","type":"journal-article","created":{"date-parts":[[2017,3,20]],"date-time":"2017-03-20T12:38:24Z","timestamp":1490013504000},"update-policy":"https:\/\/doi.org\/10.1063\/aip-crossmark-policy-page","source":"Crossref","is-referenced-by-count":19,"title":["The attachment of \u03b1-synuclein to a fiber: A coarse-grain approach"],"prefix":"10.1063","volume":"146","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5935-3332","authenticated-orcid":false,"given":"Ioana M.","family":"Ilie","sequence":"first","affiliation":[{"name":"University of Twente 1 Computational Chemical Physics, Faculty of Science and Technology, , P.O. 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