title: Long-range correlated dynamics in intrinsically disordered proteins.
abstract: 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.
authors.affiliation: Department of Chemistry "Ugo Schiff" and CERM, University of Florence , via Sacconi 6, 50019 Sesto Fiorentino, Italy.
authors.forename: Giacomo
authors.initials: G
authors.lastname: Parigi
authors.forename: Nasrollah
authors.initials: N
authors.lastname: Rezaei-Ghaleh
authors.forename: Andrea
authors.initials: A
authors.lastname: Giachetti
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Claudio
authors.initials: C
authors.lastname: Fernandez
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
authors.forename: Christian
authors.initials: C
authors.lastname: Griesinger
authors.forename: Markus
authors.initials: M
authors.lastname: Zweckstetter
authors.forename: Claudio
authors.initials: C
authors.lastname: Luchinat
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D011522:Protons; D013696:Temperature; D014867:Water / Q000737:chemistry; D051844:alpha-Synuclein / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D064267:Intrinsically Disordered Proteins; D011522:Protons; D051844:alpha-Synuclein; D014867:Water