{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T19:17:05Z","timestamp":1790623025416,"version":"4.1.0"},"reference-count":147,"publisher":"AIP Publishing","issue":"24","funder":[{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["PHY-1430124"],"award-info":[{"award-number":["PHY-1430124"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["9P41-GM104601, R01-GM067887 and U54-GM087519"],"award-info":[{"award-number":["9P41-GM104601, R01-GM067887 and U54-GM087519"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["pubs.aip.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2015,12,28]]},"abstract":"<jats:p>Parkinson\u2019s disease, originating from the intrinsically disordered peptide \u03b1-synuclein, is a common neurodegenerative disorder that affects more than 5% of the population above age 85. It remains unclear how \u03b1-synuclein monomers undergo conformational changes leading to aggregation and formation of fibrils characteristic for the disease. In the present study, we perform molecular dynamics simulations (over 180 \u03bcs in aggregated time) using a hybrid-resolution model, Proteins with Atomic details in Coarse-grained Environment (PACE), to characterize in atomic detail structural ensembles of wild type and mutant monomeric \u03b1-synuclein in aqueous solution. The simulations reproduce structural properties of \u03b1-synuclein characterized in experiments, such as secondary structure content, long-range contacts, chemical shifts, and 3J(HNHC\u03b1)-coupling constants. Most notably, the simulations reveal that a short fragment encompassing region 38-53, adjacent to the non-amyloid-\u03b2 component region, exhibits a high probability of forming a \u03b2-hairpin; this fragment, when isolated from the remainder of \u03b1-synuclein, fluctuates frequently into its \u03b2-hairpin conformation. Two disease-prone mutations, namely, A30P and A53T, significantly accelerate the formation of a \u03b2-hairpin in the stated fragment. We conclude that the formation of a \u03b2-hairpin in region 38-53 is a key event during \u03b1-synuclein aggregation. We predict further that the G47V mutation impedes the formation of a turn in the \u03b2-hairpin and slows down \u03b2-hairpin formation, thereby retarding \u03b1-synuclein aggregation.<\/jats:p>","DOI":"10.1063\/1.4936910","type":"journal-article","created":{"date-parts":[[2015,12,10]],"date-time":"2015-12-10T09:09:11Z","timestamp":1449738551000},"update-policy":"https:\/\/doi.org\/10.1063\/aip-crossmark-policy-page","source":"Crossref","is-referenced-by-count":104,"title":["Transient\n                    <i>\u03b2<\/i>\n                    -hairpin formation in\n                    <i>\u03b1<\/i>\n                    -synuclein monomer revealed by coarse-grained molecular dynamics simulation"],"prefix":"10.1063","volume":"143","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8915-2323","authenticated-orcid":false,"given":"Hang","family":"Yu","sequence":"first","affiliation":[{"name":"University of Illinois at Urbana-Champaign 1 Beckman Institute for Advanced Science and Technology, , Urbana, Illinois 61801, USA"},{"name":"University of Illinois at Urbana-Champaign 2 Center for Biophysics and Computational Biology, , Urbana, Illinois 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei","family":"Han","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign 1 Beckman Institute for Advanced Science and Technology, , Urbana, Illinois 61801, USA"},{"name":"University of Illinois at Urbana-Champaign 3 Department of Physics, , Urbana, Illinois 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wen","family":"Ma","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign 1 Beckman Institute for Advanced Science and Technology, , Urbana, Illinois 61801, USA"},{"name":"University of Illinois at Urbana-Champaign 2 Center for Biophysics and Computational Biology, , Urbana, Illinois 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Schulten","sequence":"additional","affiliation":[{"name":"University of Illinois at Urbana-Champaign 1 Beckman Institute for Advanced Science and Technology, , Urbana, Illinois 61801, USA"},{"name":"University of Illinois at Urbana-Champaign 2 Center for Biophysics and Computational Biology, , Urbana, Illinois 61801, USA"},{"name":"University of Illinois at Urbana-Champaign 3 Department of Physics, , Urbana, Illinois 61801, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"317","published-online":{"date-parts":[[2015,12,9]]},"reference":[{"key":"2023080307573787100_c1","doi-asserted-by":"publisher","first-page":"1255555","DOI":"10.1126\/science.1255555","article-title":"Alzheimer\u2019s and Parkinson\u2019s diseases: The prion concept in relation to assembled A\u03b2, tau, and \u03b1-synuclein","volume":"349","year":"2015","journal-title":"Science"},{"key":"2023080307573787100_c2","first-page":"879","article-title":"Aggregation of \u03b1-synuclein in Lewy bodies of sporadic Parkinson\u2019s disease and dementia with Lewy bodies","volume":"152","year":"1998","journal-title":"Am. 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