Krigbaum W R, Komoriya A
Biochim Biophys Acta. 1979 Jan 25;576(1):204-48. doi: 10.1016/0005-2795(79)90498-7.
Van der Waals interactions between sidechains are indicated to be important in determining the native state of the proteins of known structure by the following observations: 1. the average radial distribution of polarity increases continuously from the center of the molecule to its periphery. 2. nonpolar sidechains tend to occur in clusters. 3. the frequencies of long-range nearest-neighbor pairs are markedly non-random; each type of sidechain seeks nearest-neighbors of similar polarity. To investigate how these interactions affect the overall structure of the protein molecule, three simplified models are treated: a sheath-core model composed of independent residues, a modification accounting approximately for the connected nature of the chain, and a model consisting of three concentric spherical phases.
通过以下观察结果表明，侧链之间的范德华相互作用在确定已知结构蛋白质的天然状态中很重要：1. 极性的平均径向分布从分子中心到其外围持续增加。2. 非极性侧链倾向于成簇出现。3. 长程最近邻对的频率明显是非随机的；每种类型的侧链都寻找极性相似的最近邻。为了研究这些相互作用如何影响蛋白质分子的整体结构，对三种简化模型进行了处理：由独立残基组成的鞘-核模型、大致考虑链的连接性质的修正模型以及由三个同心球相组成的模型。
