TY  - JOUR
AU  - Parigi, Giacomo
AU  - Rezaei-Ghaleh, Nasrollah
AU  - Giachetti, Andrea
AU  - Becker, Stefan
AU  - Fernandez, Claudio
AU  - Blackledge, Martin
AU  - Griesinger, Christian
AU  - Zweckstetter, Markus
AU  - Luchinat, Claudio
TI  - Long-range correlated dynamics in intrinsically disordered proteins.
JO  - Journal of the American Chemical Society
VL  - 136
IS  - 46
SN  - 0002-7863
CY  - Washington, DC
PB  - American Chemical Society
M1  - DZNE-2020-03968
SP  - 16201-16209
PY  - 2014
AB  - 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.
KW  - Animals
KW  - Chemical Phenomena
KW  - Intrinsically Disordered Proteins: chemistry
KW  - Intrinsically Disordered Proteins: genetics
KW  - Intrinsically Disordered Proteins: metabolism
KW  - Models, Molecular
KW  - Mutation
KW  - Protein Conformation
KW  - Protons
KW  - Temperature
KW  - Water: chemistry
KW  - alpha-Synuclein: chemistry
KW  - alpha-Synuclein: genetics
KW  - alpha-Synuclein: metabolism
KW  - Intrinsically Disordered Proteins (NLM Chemicals)
KW  - Protons (NLM Chemicals)
KW  - alpha-Synuclein (NLM Chemicals)
KW  - Water (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:25331250
DO  - DOI:10.1021/ja506820r
UR  - https://pub.dzne.de/record/137646
ER  -