Role of explicitly cooperative interactions in protein folding funnels: A simulation study
Role of explicitly cooperative interactions in protein folding funnels: A simulation study
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DOI：
10.1063/1.1315994
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发表时间：
2001-03-08
影响因子：
4.4
通讯作者：
Wolynes, PG
中科院分区：
文献类型：
--
作者：
Eastwood, MP;Wolynes, PG
我们讨论了一个包含非成对可加相互作用的模型蛋白质的非晶格模拟。确定了在物理上合理的范围内改变非加性强度对折叠漏斗形貌的影响，即自由能分布作为全局和局域有序参数的函数。与现有的基于能量景观思想的自由能剖面理论进行了关键的比较。虽然全球平均场理论给出了基本模拟结果的正确趋势，但它的势垒对于短程相互作用并不是定量准确的。允许序参数在空间上变化的变分近似提供了相当精确的势垒和有序局域化的准确图像。(C)2001年美国物理研究所。
We discuss an off-lattice simulation of a model protein containing nonpairwise-additive interactions. The effect of varying the strength of nonadditivity within a physically reasonable range on the folding funnel topography, i.e., free energy profiles as a function of global and local order parameters, is determined. A critical comparison is made with existing theories of free energy profiles based on energy landscape ideas. While the global mean-field theory gives the correct trends for the essential simulation results, its barriers are not quantitatively accurate for short range interactions. Variational approximations that allow spatial variation of the order parameter provide quite accurate barriers and accurate pictures of the localization of order. (C) 2001 American Institute of Physics.