Jiang S, Vakser I A
Department of Cell and Molecular Pharmacology, Medical University of South Carolina, Charleston, South Carolina 29425, USA.
Proteins. 2000 Aug 15;40(3):429-35. doi: 10.1002/1097-0134(20000815)40:3<429::aid-prot80>3.0.co;2-2.
Transmembrane helices from crystallographically determined structures were analyzed to determine the distribution of side chains inside and outside helix-helix interfaces. Two structural characteristics were explored: (1) the number of atoms outside the interfaces that belong to the side chains with the C(alpha) atoms inside the interfaces, as well as the opposite, inside/outside number (conformation-dependent values) and (2) the side-chain length (depends only on the residue type and does not depend on the side-chain conformation). The results showed that the interface side chains tend to be bent away from the interacting helix. The most important finding, however, is that the side chains in the interface areas, on average, are shorter than in the noninterface areas. Proteins 2000;40:429-435.
对晶体学确定结构中的跨膜螺旋进行了分析，以确定螺旋-螺旋界面内外侧链的分布。研究了两个结构特征：（1）界面外属于侧链且其Cα原子在界面内的原子数，以及相反情况，即内侧/外侧数（构象相关值）；（2）侧链长度（仅取决于残基类型，不取决于侧链构象）。结果表明，界面侧链倾向于从相互作用的螺旋处弯曲离开。然而，最重要的发现是，界面区域的侧链平均比非界面区域的侧链短。《蛋白质2000》；40：429 - 435。
