%0 Journal Article
%A Parigi, Giacomo
%A Rezaei-Ghaleh, Nasrollah
%A Giachetti, Andrea
%A Becker, Stefan
%A Fernandez, Claudio
%A Blackledge, Martin
%A Griesinger, Christian
%A Zweckstetter, Markus
%A Luchinat, Claudio
%T Long-range correlated dynamics in intrinsically disordered proteins.
%J Journal of the American Chemical Society
%V 136
%N 46
%@ 0002-7863
%C Washington, DC
%I American Chemical Society
%M DZNE-2020-03968
%P 16201-16209
%D 2014
%X 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.
%K Animals
%K Chemical Phenomena
%K Intrinsically Disordered Proteins: chemistry
%K Intrinsically Disordered Proteins: genetics
%K Intrinsically Disordered Proteins: metabolism
%K Models, Molecular
%K Mutation
%K Protein Conformation
%K Protons
%K Temperature
%K Water: chemistry
%K alpha-Synuclein: chemistry
%K alpha-Synuclein: genetics
%K alpha-Synuclein: metabolism
%K Intrinsically Disordered Proteins (NLM Chemicals)
%K Protons (NLM Chemicals)
%K alpha-Synuclein (NLM Chemicals)
%K Water (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:25331250
%R 10.1021/ja506820r
%U https://pub.dzne.de/record/137646