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001     137646
005     20240321220303.0
024 7 _ |a 10.1021/ja506820r
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024 7 _ |a pmid:25331250
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024 7 _ |a 0002-7863
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024 7 _ |a 1520-5126
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024 7 _ |a 1943-2984
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037 _ _ |a DZNE-2020-03968
041 _ _ |a English
082 _ _ |a 540
100 1 _ |a Parigi, Giacomo
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245 _ _ |a Long-range correlated dynamics in intrinsically disordered proteins.
260 _ _ |a Washington, DC
|c 2014
|b American Chemical Society
264 _ 1 |3 online
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|b American Chemical Society (ACS)
|c 2014-11-04
264 _ 1 |3 print
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|b American Chemical Society (ACS)
|c 2014-11-19
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520 _ _ |a Intrinsically 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.
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650 _ 7 |a Intrinsically Disordered Proteins
|2 NLM Chemicals
650 _ 7 |a Protons
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650 _ 7 |a alpha-Synuclein
|2 NLM Chemicals
650 _ 7 |a Water
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650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Chemical Phenomena
|2 MeSH
650 _ 2 |a Intrinsically Disordered Proteins: chemistry
|2 MeSH
650 _ 2 |a Intrinsically Disordered Proteins: genetics
|2 MeSH
650 _ 2 |a Intrinsically Disordered Proteins: metabolism
|2 MeSH
650 _ 2 |a Models, Molecular
|2 MeSH
650 _ 2 |a Mutation
|2 MeSH
650 _ 2 |a Protein Conformation
|2 MeSH
650 _ 2 |a Protons
|2 MeSH
650 _ 2 |a Temperature
|2 MeSH
650 _ 2 |a Water: chemistry
|2 MeSH
650 _ 2 |a alpha-Synuclein: chemistry
|2 MeSH
650 _ 2 |a alpha-Synuclein: genetics
|2 MeSH
650 _ 2 |a alpha-Synuclein: metabolism
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700 1 _ |a Rezaei-Ghaleh, Nasrollah
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700 1 _ |a Giachetti, Andrea
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700 1 _ |a Becker, Stefan
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700 1 _ |a Fernandez, Claudio
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700 1 _ |a Blackledge, Martin
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700 1 _ |a Griesinger, Christian
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700 1 _ |a Zweckstetter, Markus
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|e Corresponding author
700 1 _ |a Luchinat, Claudio
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773 1 8 |a 10.1021/ja506820r
|b : American Chemical Society (ACS), 2014-11-04
|n 46
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|t Journal of the American Chemical Society
|v 136
|y 2014
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773 _ _ |a 10.1021/ja506820r
|g Vol. 136, no. 46, p. 16201 - 16209
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856 4 _ |u https://pubs.acs.org/doi/10.1021/ja506820r
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