Head-Gordon T, Stillinger F H, Arrecis J
AT&T Bell Laboratories, Murray Hill, NJ 07974.
Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11076-80. doi: 10.1073/pnas.88.24.11076.
Locating the native structure of a given protein is a task made difficult by the complexity of the potential energy hypersurface and by the huge number of local minima it contains. We have explored a strategy (the "antlion" method) for hypersurface modification that suppresses all minima but that of the native structure. Transferrable penalty functions with general applicability for modifying a hypersurface to retain the desired minimum are identified, and two blocked oligopeptides (alanine dipeptide and tetrapeptide) are used for specific numerical illustration of the dramatic simplification that ensues. In addition, an intermediary role for neural networks to manage some aspects of the antlion strategy applied to large polypeptides and proteins is introduced.
确定给定蛋白质的天然结构是一项艰巨的任务，这是由于势能超曲面的复杂性以及它所包含的大量局部最小值。我们探索了一种用于超曲面修饰的策略（“蚁狮”方法），该方法可以抑制除天然结构最小值之外的所有最小值。确定了具有普遍适用性的可转移惩罚函数，用于修饰超曲面以保留所需的最小值，并使用两种受阻寡肽（丙氨酸二肽和四肽）对由此产生的显著简化进行了具体的数值说明。此外，还引入了神经网络在管理应用于大型多肽和蛋白质的蚁狮策略的某些方面所起的中介作用。
