STRUCTURAL INVARIANTS IN PROTEIN FOLDING
STRUCTURAL INVARIANTS IN PROTEIN FOLDING
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DOI：
10.1038/254304a0
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发表时间：
1975-01-01
期刊：
影响因子：
64.8
通讯作者：
CHOTHIA, C
中科院分区：
文献类型：
--
作者：
CHOTHIA, C
对 15 种蛋白质结构的分析表明：首先，单体蛋白质折叠时可及表面积的损失（与疏水能量成正比）是分子量的简单函数；第二，形成分子内氢键的极性基团比例恒定；第三，蛋白质内部紧密堆积，每个残基所占的体积与氨基酸晶体中的体积相同。
An analysis of 15 protein structures indicates: First, the loss of accessible surface area by monomeric proteins on folding—proportional to hydrophobic energy—is a simple function of molecular weight; second, the proportion of polar groups forming intramolecular hydrogen bonds is constant; and third, protein interiors are closely packed, each residue occupying the same volume as it does in crystals of amino acids.