期刊
NATURE PHYSICS
卷 12, 期 2, 页码 171-174出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NPHYS3553
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资金
- National Institutes of Health (NIH) [P41GM103712-S1]
- Pittsburgh Supercomputing Center (PSC) [P41GM103712-S1]
- Office of Science of the US Department of Energy [DE-AC05-00OR22725, DE-AC02-05CH11231]
- NSF China [11504231]
Internal motions of proteins are essential to their function. The time dependence of protein structural fluctuations is highly complex, manifesting subdiffusive, non-exponential behaviour with effective relaxation times existing over many decades in time, from ps up to similar to 10(2) s (refs 1-4). Here, using molecular dynamics simulations, we show that, on timescales from 10(-12) to 10(-5) s, motions in single proteins are self-similar, non-equilibrium and exhibit ageing. The characteristic relaxation time for a distance fluctuation, such as inter-domain motion, is observation-time-dependent, increasing in a simple, power-law fashion, arising from the fractal nature of the topology and geometry of the energy landscape explored. Diffusion over the energy landscape follows a non-ergodic continuous time random walk. Comparison with single-molecule experiments suggests that the non-equilibrium self-similar dynamical behaviour persists up to timescales approaching the in vivo lifespan of individual protein molecules.
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