Artículos de revistas
Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
Fecha
2014-10Registro en:
Parigi, Giacomo; Rezaei Ghaleh, Nasrollah; Giachetti, Andrea; Becker, Stefan; Fernandez, Claudio Oscar; et al.; Long-Range Correlated Dynamics in Intrinsically Disordered Proteins; American Chemical Society; Journal of the American Chemical Society; 136; 10-2014; 16201-16209
0002-7863
CONICET Digital
CONICET
Autor
Parigi, Giacomo
Rezaei Ghaleh, Nasrollah
Giachetti, Andrea
Becker, Stefan
Fernandez, Claudio Oscar
Blackledger, Martin
Griesinger, Christian
Zweckstetter, Markus
Luchinat, Claudio
Resumen
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