Vtyurin N, Panov V
Department of Biopolymers Structure and Function Research, Russian Academy of Sciences, Moscow.
Proteins. 1995 Mar;21(3):256-60. doi: 10.1002/prot.340210308.
An analysis of possible tight packing of hydrophobic groups simultaneously at the both surfaces of beta-hyperboloid-8 was conducted. This analysis shows that the disposition of amino acid side chains at the real beta-structure's surface is unique. If we sign the mean distance between adjacent beta-strands as "a," and the mean distance along beta-strand between C alpha atoms, whose side chains are directed to one side of the beta-sheet, as "b," the ratio b/a = square root of 2 very precisely. This ratio ensures the most efficient packing of side hydrophobic groups at the outer surface of beta-hyperboloid-8, forming, at the same time, the second by efficiency packing at its inner surface.
对β-双曲面-8两个表面同时存在的疏水基团可能的紧密堆积进行了分析。该分析表明，在真实β结构表面氨基酸侧链的排布是独特的。如果将相邻β链之间的平均距离记为“a”，将其侧链指向β折叠一侧的Cα原子沿β链之间的平均距离记为“b”，那么b/a = √2，精度非常高。该比例确保了β-双曲面-8外表面侧疏水基团的最有效堆积，同时在其内表面形成效率第二高的堆积。
