000169187 001__ 169187
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000169187 0247_ $$2doi$$a10.1002/chem.202203493
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000169187 041__ $$aEnglish
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000169187 1001_ $$0P:(DE-2719)9001298$$aAbyzov, Anton$$b0
000169187 245__ $$aFast Motions Dominate Dynamics of Intrinsically Disordered Tau Protein at High Temperatures.
000169187 260__ $$aWeinheim$$bWiley-VCH$$c2023
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000169187 520__ $$a Reorientational dynamics of intrinsically disordered proteins (IDPs) contain multiple motions often clustered around three motional modes: ultrafast librational motions of amide groups, fast local backbone conformational fluctuations and slow chain segmental motions. This dynamic picture is mainly based on 15 N NMR relaxation studies of IDPs at relatively low temperatures where the amide-water proton exchange rates are sufficiently small. Less is known, however, about the dynamics of IDPs at more physiological temperatures. Here, we investigate protein dynamics in a 441-residue long IDP, tau protein, in the temperature range from 0-25 °C, using 15 N NMR relaxation rates and spectral density analysis. While at these temperatures relaxation rates are still better described in terms of amide group librational motions, local backbone dynamics and chain segmental motions, the temperature-dependent trend of spectral densities suggests that the timescales of fast backbone conformational fluctuations and slower chain segmental motions might become inseparable at higher temperatures. Our data demonstrate the remarkable dynamic plasticity of this prototypical IDP and highlight the need for dynamic studies of IDPs at multiple temperatures.
000169187 536__ $$0G:(DE-HGF)POF4-352$$a352 - Disease Mechanisms (POF4-352)$$cPOF4-352$$fPOF IV$$x0
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000169187 650_2 $$2MeSH$$aTemperature
000169187 650_2 $$2MeSH$$aProtein Conformation
000169187 650_2 $$2MeSH$$atau Proteins
000169187 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy
000169187 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: chemistry
000169187 650_2 $$2MeSH$$aAmides
000169187 650_7 $$2NLM Chemicals$$atau Proteins
000169187 650_7 $$2Other$$aIntrinsically disordered protein
000169187 650_7 $$2Other$$aNMR relaxation
000169187 650_7 $$2Other$$aprotein dynamics
000169187 650_7 $$2Other$$aspectral density analysis
000169187 650_7 $$2Other$$atau protein
000169187 650_7 $$2NLM Chemicals$$aIntrinsically Disordered Proteins
000169187 650_7 $$2NLM Chemicals$$aAmides
000169187 7001_ $$0P:(DE-2719)2541671$$aMandelkow, Eckhard$$b1
000169187 7001_ $$0P:(DE-2719)2810591$$aZweckstetter, Markus$$b2
000169187 7001_ $$0P:(DE-2719)9000418$$aRezaei-Ghaleh, Nasrollah$$b3$$eCorresponding author
000169187 773__ $$0PERI:(DE-600)1478547-X$$a10.1002/chem.202203493$$gp. chem.202203493$$n17$$pe202203493$$tChemistry - a European journal$$v29$$x0947-6539$$y2023
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000169187 9141_ $$y2023
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000169187 9201_ $$0I:(DE-2719)1013014$$kAG Mandelkow 1$$lStructural Principles of Neurodegeneration$$x0
000169187 9201_ $$0I:(DE-2719)1410001$$kAG Zweckstetter$$lStructural Biology in Dementia$$x1
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