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000137646 0247_ $$2doi$$a10.1021/ja506820r
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000137646 0247_ $$2ISSN$$a0002-7863
000137646 0247_ $$2ISSN$$a1520-5126
000137646 0247_ $$2ISSN$$a1943-2984
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000137646 037__ $$aDZNE-2020-03968
000137646 041__ $$aEnglish
000137646 082__ $$a540
000137646 1001_ $$0P:(DE-HGF)0$$aParigi, Giacomo$$b0
000137646 245__ $$aLong-range correlated dynamics in intrinsically disordered proteins.
000137646 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2014
000137646 264_1 $$2Crossref$$3online$$bAmerican Chemical Society (ACS)$$c2014-11-04
000137646 264_1 $$2Crossref$$3print$$bAmerican Chemical Society (ACS)$$c2014-11-19
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000137646 520__ $$aIntrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in α-synuclein, which are related to genetic forms of Parkinson's disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems.
000137646 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000137646 650_7 $$2NLM Chemicals$$aIntrinsically Disordered Proteins
000137646 650_7 $$2NLM Chemicals$$aProtons
000137646 650_7 $$2NLM Chemicals$$aalpha-Synuclein
000137646 650_7 $$0059QF0KO0R$$2NLM Chemicals$$aWater
000137646 650_2 $$2MeSH$$aAnimals
000137646 650_2 $$2MeSH$$aChemical Phenomena
000137646 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: chemistry
000137646 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: genetics
000137646 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: metabolism
000137646 650_2 $$2MeSH$$aModels, Molecular
000137646 650_2 $$2MeSH$$aMutation
000137646 650_2 $$2MeSH$$aProtein Conformation
000137646 650_2 $$2MeSH$$aProtons
000137646 650_2 $$2MeSH$$aTemperature
000137646 650_2 $$2MeSH$$aWater: chemistry
000137646 650_2 $$2MeSH$$aalpha-Synuclein: chemistry
000137646 650_2 $$2MeSH$$aalpha-Synuclein: genetics
000137646 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000137646 7001_ $$0P:(DE-2719)9000418$$aRezaei-Ghaleh, Nasrollah$$b1$$udzne
000137646 7001_ $$0P:(DE-HGF)0$$aGiachetti, Andrea$$b2
000137646 7001_ $$0P:(DE-HGF)0$$aBecker, Stefan$$b3
000137646 7001_ $$0P:(DE-HGF)0$$aFernandez, Claudio$$b4
000137646 7001_ $$0P:(DE-HGF)0$$aBlackledge, Martin$$b5
000137646 7001_ $$0P:(DE-HGF)0$$aGriesinger, Christian$$b6
000137646 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b7$$eCorresponding author
000137646 7001_ $$0P:(DE-HGF)0$$aLuchinat, Claudio$$b8
000137646 77318 $$2Crossref$$3journal-article$$a10.1021/ja506820r$$b : American Chemical Society (ACS), 2014-11-04$$n46$$p16201-16209$$tJournal of the American Chemical Society$$v136$$x0002-7863$$y2014
000137646 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/ja506820r$$gVol. 136, no. 46, p. 16201 - 16209$$n46$$p16201-16209$$q136:46<16201 - 16209$$tJournal of the American Chemical Society$$v136$$x0002-7863$$y2014
000137646 8564_ $$uhttps://pubs.acs.org/doi/10.1021/ja506820r
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