SURFACE AND INSIDE VOLUMES IN GLOBULAR PROTEINS
SURFACE AND INSIDE VOLUMES IN GLOBULAR PROTEINS
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DOI：
10.1038/277491a0
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发表时间：
1979-01-01
期刊：
影响因子：
64.8
通讯作者：
JANIN, J
中科院分区：
文献类型：
--
作者：
JANIN, J
对溶剂可及的表面积的测量提供了已知X射线结构的蛋白质的表面和内部体积的方便定义。对几种蛋白质中氨基酸残基溶剂可及性的研究1 -3证实了早期的观察结果，即极性残基主要存在于表面，非极性残基主要存在于球状蛋白质结构内部。但由于表面积与体积比的变化，可及性随分子量的变化而表现出系统的变化。实验数据4表明，单体球状蛋白质的可及表面积A（单位：μ 2）遵循定律5，6：这意味着每个残基的平均可及表面积随着M的增加而减少，如M− 1/3（其中M是分子量），从分子量为6，000的蛋白质的约68 μ 2减少到分子量为35，000的蛋白质的38 μ 2。因此，对溶剂的可及性不是氨基酸的特征。
MEASUREMENTS of the surface area accessible to solvent provide a convenient definition of the surface and the inside volumes in proteins of known X-ray structure. The study of the accessibility to solvent of amino acid residues in several proteins1–3 has confirmed the early observation that polar residues are found mostly on the surface and non-polar residues mostly inside globular protein structures. But the accessibility shows systematic variations with the molecular weight, because of the change in surface to volume ratio. Experimental data4 indicate that the accessible surface area A (in Å2) of monomeric globular proteins follows the law5, 6: which implies that the mean accessible surface area per residues decreases like M− 1/3 (where M is molecular weight) with increasing M, from about 68 Å2 for proteins of 6,000 molecular weight to 38 Å2 for proteins of 35,000 molecular weight. Thus, the accessibility to solvent is not a characteristic of the amino acids.