{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T09:08:16Z","timestamp":1789895296216,"version":"4.0.1"},"reference-count":137,"publisher":"American Chemical Society (ACS)","issue":"46","license":[{"start":{"date-parts":[[2015,10,28]],"date-time":"2015-10-28T00:00:00Z","timestamp":1445990400000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000275","name":"Leverhulme Trust","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000275","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Woolf Fisher Trust","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,11,25]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\u03b1-Synuclein is an intrinsically disordered protein whose aggregation is implicated in Parkinson\u2019s disease. A second member of the synuclein family, \u03b2-synuclein, shares significant sequence similarity with \u03b1-synuclein but is much more resistant to aggregation. \u03b2-Synuclein is missing an 11-residue stretch in the central non-\u03b2-amyloid component region that forms the core of \u03b1-synuclein amyloid fibrils, yet insertion of these residues into \u03b2-synuclein to produce the \u03b2SHC construct does not markedly increase the aggregation propensity. To investigate the structural basis of these different behaviors, quantitative nuclear magnetic resonance data, in the form of paramagnetic relaxation enhancement-derived interatomic distances, are combined with molecular dynamics simulations to generate ensembles of structures representative of the solution states of \u03b1-synuclein, \u03b2-synuclein, and \u03b2SHC. Comparison of these ensembles reveals that the differing aggregation propensities of \u03b1-synuclein and \u03b2-synuclein are associated with differences in the degree of residual structure in the C-terminus coupled to the shorter separation between the N- and C-termini in \u03b2-synuclein and \u03b2SHC, making protective intramolecular contacts more likely.<\/jats:p>","DOI":"10.1021\/bi5009326","type":"journal-article","created":{"date-parts":[[2014,10,28]],"date-time":"2014-10-28T17:23:22Z","timestamp":1414517002000},"page":"7170-7183","source":"Crossref","is-referenced-by-count":62,"title":["A Relationship between the Transient Structure in\nthe Monomeric State and the Aggregation Propensities of \u03b1-Synuclein\nand \u03b2-Synuclein"],"prefix":"10.1021","volume":"53","author":[{"given":"Jane R.","family":"Allison","sequence":"first","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert C.","family":"Rivers","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John C.","family":"Christodoulou","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michele","family":"Vendruscolo","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher M.","family":"Dobson","sequence":"additional","affiliation":[{"name":"University of Cambridge , , Lensfield Road , ,","place":["Cambridge, U.K., CB2 1EW"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,10,28]]},"reference":[{"key":"2026090117345610900_cit1","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/nrm1589","article-title":"Intrinsically unstructured proteins and their functions","volume":"6","author":"Dyson","year":"2005","journal-title":"Nat. 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