期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 17, 期 2, 页码 762-782出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4cp03058c
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资金
- NIH
- BBSRC
- Biotechnology and Biological Sciences Research Council [BB/K016245/1, BBS/B/10218] Funding Source: researchfish
- BBSRC [BB/K016245/1] Funding Source: UKRI
Although protein folding is often described by motion on a funnel-shaped overall topology of the energy landscape, the many local interactions that can occur result in considerable landscape roughness which slows folding by increasing internal friction. Recent experimental results have brought to light that this roughness also causes unusual diffusional behaviour of the backbone of an unfolded protein, i.e. the relative motion of protein sections cannot be described by the normal diffusion equation, but shows strongly subdiffusional behaviour with a nonlinear time dependence of the mean square displacement, (r(2)(t) proportional to t(alpha) (alpha << 1). This results in significantly slower configurational equilibration than had been assumed hitherto. Analysis of the results also allows quantification of the energy landscape roughness, i.e. the root-mean-squared depth of local minima, yielding a value of 4-5k(B)T for a typical small protein.
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