从头设计的螺旋蛋白的计算机模拟。
Computer simulations of de novo designed helical proteins.
作者信息
Sikorski A, Kolinski A, Skolnick J
机构信息
Department of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
出版信息
Biophys J. 1998 Jul;75(1):92-105. doi: 10.1016/S0006-3495(98)77497-1.
In the context of reduced protein models, Monte Carlo simulations of three de novo designed helical proteins (four-member helical bundle) were performed. At low temperatures, for all proteins under consideration, protein-like folds having different topologies were obtained from random starting conformations. These simulations are consistent with experimental evidence indicating that these de novo designed proteins have the features of a molten globule state. The results of Monte Carlo simulations suggest that these molecules adopt four-helix bundle topologies. They also give insight into the possible mechanism of folding and association, which occurs in these simulations by on-site assembly of the helices. The low-temperature conformations of all three sequences have the features of a molten globule state.
在简化蛋白质模型的背景下，对三种从头设计的螺旋蛋白（四螺旋束）进行了蒙特卡罗模拟。在低温下，对于所有考虑的蛋白质，从随机起始构象中获得了具有不同拓扑结构的类蛋白质折叠。这些模拟与实验证据一致，表明这些从头设计的蛋白质具有熔球态的特征。蒙特卡罗模拟结果表明这些分子采用四螺旋束拓扑结构。它们还深入了解了折叠和缔合的可能机制，这种机制在这些模拟中通过螺旋的原位组装发生。所有三个序列的低温构象都具有熔球态的特征。
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