The contacts between bulky hydrophobic side chains (Val, Leu, Ile, Met, Phe, Tyr, and Trp) were studied in five globins with known three-dimensional structures. It is shown that a large majority of these side chains participate in such contacts, where most often one side chain makes contact with two to four nearby side chains. The "recognition element" of a helical region is most often a pair of bulky hydrophobic side chains belinging to neighboring turns of an alpha-helix. Such pairs most often make contact with bulky hydrophobic side chains brought in from the outside. An analysis is made of contacts between the hydrophobic side chains common to all five globins. It is shown that as a rule the most intense contacts in each globin are also common to the five globins. The role of these invariant contacts in the formation of the tertiary structure of globin molecules is considered. A suggestion is made that the apoglobin molecule consists of independently self-organizing halves, the internal structure of which is less subject to fluctuation than their mutual arrangement.

中文翻译：

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珠蛋白的疏水核的结构。

在具有已知三维结构的五种球蛋白中研究了庞大的疏水性侧链（Val，Leu，Ile，Met，Phe，Tyr和Trp）之间的接触。结果表明，这些侧链中的绝大多数都参与了这种接触，其中最经常的是一个侧链与附近的两到四个侧链接触。螺旋区的“识别元件”最常见的是一对笨重的疏水侧链，它们紧靠α-螺旋的相邻匝。这种对最常与从外部引入的庞大的疏水性侧链接触。对所有五个球蛋白共有的疏水性侧链之间的接触进行了分析。结果表明，通常每个珠蛋白中最紧密的接触也是五个珠蛋白所共有的。考虑了这些不变接触在珠蛋白分子三级结构形成中的作用。有人提出，载脂蛋白分子由独立的自组织半体组成，其内部结构比相互排列更容易受到波动的影响。