Lovejoy B, Choe S, Cascio D, McRorie D K, DeGrado W F, Eisenberg D
Molecular Biology Institute, University of California, Los Angeles 90024-1570.
Science. 1993 Feb 26;259(5099):1288-93. doi: 10.1126/science.8446897.
The x-ray crystal structure of a peptide designed to form a double-stranded parallel coiled coil shows that it is actually a triple-stranded coiled coil formed by three alpha-helices. Unlike the designed parallel coiled coil, the helices run up-up-down. The structure is stabilized by a distinctive hydrophobic interface consisting of eight layers. As in the design, each alpha-helix in the coiled coil contributes one leucine side chain to each layer. The structure suggests that hydrophobic interactions are a dominant factor in the stabilization of coiled coils. The stoichiometry and geometry of coiled coils are primarily determined by side chain packing in the solvent-inaccessible interior, but electrostatic interactions also contribute.
一种设计成形成双链平行卷曲螺旋的肽的X射线晶体结构表明，它实际上是由三个α螺旋形成的三链卷曲螺旋。与设计的平行卷曲螺旋不同，这些螺旋是向上-向上-向下排列的。该结构由一个由八层组成的独特疏水界面稳定。与设计中一样，卷曲螺旋中的每个α螺旋为每层贡献一个亮氨酸侧链。该结构表明疏水相互作用是卷曲螺旋稳定的主要因素。卷曲螺旋的化学计量和几何形状主要由溶剂不可及内部的侧链堆积决定，但静电相互作用也有贡献。
