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Here we studied the structural consequences upon binding of the repeat domain of Tau, which plays a key role in pathogenic aggregation, to an aggregation enhancer. By combining NMR experiments with molecular simulations we show that binding of the aggregation enhancer polyglutamic acid remodels the conformational ensemble of Tau. Our study thus provides insight into an early event during misfolding of Tau.<\/jats:p>","DOI":"10.1002\/pro.2911","type":"journal-article","created":{"date-parts":[[2016,3,5]],"date-time":"2016-03-05T16:06:05Z","timestamp":1457193965000},"page":"1010-1020","source":"Crossref","is-referenced-by-count":33,"title":["Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer"],"prefix":"10.1002","volume":"25","author":[{"given":"Elias","family":"Akoury","sequence":"first","affiliation":[{"name":"Department for NMR\u2010based Structural Biology Max Planck Institute for Biophysical Chemistry G\u00f6ttingen 37077 Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marco D.","family":"Mukrasch","sequence":"additional","affiliation":[{"name":"Department for NMR\u2010based Structural Biology Max Planck Institute for Biophysical Chemistry G\u00f6ttingen 37077 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