Long-Range Correlated Dynamics in Intrinsically Disordered Proteins
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- 作者：Giacomo Parigi ; Nasrollah Rezaei-Ghaleh ; Andrea Giachetti ; Stefan Becker ; Claudio Fernandez ; Martin Blackledge ; Christian Griesinger ; Markus Zweckstetter ; Claudio Luchinat
- 刊名：Journal of the American Chemical Society
- 出版年：2014
- 出版时间：November 19, 2014
- 年：2014
- 卷：136
- 期：46
- 页码：16201-16209
- 全文大小：457K
- ISSN：1520-5126
文摘
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 伪-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 伪-synuclein, which are related to genetic forms of Parkinson鈥檚 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.