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.

Long-Range Correlated Dynamics in Intrinsically Disordered Proteins / Giacomo Parigi;Nasrollah Rezaei-Ghaleh;Andrea Giachetti;Stefan Becker;Claudio Fernandez;Martin Blackledge;Christian Griesinger;Markus Zweckstetter;Claudio Luchinat. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 136:(2014), pp. 16201-16209. [10.1021/ja506820r]

Long-Range Correlated Dynamics in Intrinsically Disordered Proteins

PARIGI, GIACOMO;GIACHETTI, ANDREA;LUCHINAT, CLAUDIO
2014

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.
2014
136
16201
16209
Giacomo Parigi;Nasrollah Rezaei-Ghaleh;Andrea Giachetti;Stefan Becker;Claudio Fernandez;Martin Blackledge;Christian Griesinger;Markus Zweckstetter;Claudio Luchinat
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/947555
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