H-P模型中具有唯一最优折叠的长链蛋白质
Long Proteins with Unique Optimal Foldings in the H-P Model
摘要：
人们普遍认为：（1）蛋白质的自然或折叠状态是一个全局能量最小值，（2）在大多数情况下，蛋白质折叠到由其氨基酸序列决定的独特状态。H-P（疏水-亲水）模型是一个简单的组合模型，旨在回答有关蛋白质折叠过程的定性问题。在本文中，我们考虑的问题提出了布赖恩海耶斯在1998年：什么蛋白质在二维H-P模型有唯一的最佳（最低能量）折叠？特别是，我们证明，有封闭的链的单体（氨基酸）具有这种属性的所有（甚至）的长度;和有开放的单体链具有这种属性的所有长度可被四除尽。
英文摘要：
It is widely accepted that (1) the natural or folded state of proteins is a global energy minimum, and (2) in most cases proteins fold to a unique state determined by their amino acid sequence. The H-P (hydrophobic-hydrophilic) model is a simple combinatorial model designed to answer qualitative questions about the protein folding process. In this paper we consider a problem suggested by Brian Hayes in 1998: what proteins in the two-dimensional H-P model have unique optimal (minimum energy) foldings? In particular, we prove that there are closed chains of monomers (amino acids) with this property for all (even) lengths; and that there are open monomer chains with this property for all lengths divisible by four.
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