NATURE OF ACCESSIBLE AND BURIED SURFACES IN PROTEINS
NATURE OF ACCESSIBLE AND BURIED SURFACES IN PROTEINS
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DOI：
10.1016/0022-2836(76)90191-1
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发表时间：
1976-01-01
影响因子：
5.6
通讯作者：
CHOTHIA, C
中科院分区：
文献类型：
--
作者：
CHOTHIA, C
计算了12种蛋白质中单个残基的可达表面积，以及6种蛋白质的延伸链、二级结构和三级结构的可达表面积。的形成。-螺旋和。beta。-由延伸链形成的褶状薄片比非极性片埋下更大比例的极性表面，并提供2-3千卡/摩尔的疏水自由能/残留物。埋在二级结构之间的表面是非常疏水的，2/3是非极性的，超过1/2的极性部分是由它们自己的二级结构内部的氢键形成的，或者是部分可以被溶剂接触到的。随着6种蛋白质分子量的增加，它们的非极性表面的埋藏比例增加（60-79%），极性表面的埋藏比例不变（75%）。讨论了这些结果对蛋白质结构理论的意义。附录显示，折叠蛋白质的可接近表面积与它们的分子量的2/3次方成正比。
The accessible surface areas were calculated for the individual residues in 12 proteins, and for the extended chains, the secondary structures and tertiary structure of 6 proteins. The formation of .alpha.-helices and .beta.-pleated sheets from an extended chain buries a greater proportion of polar surface than non-polar and gives 2-3 kcal/mol of hydrophobic free energy/residue. The surfaces buried between the secondary structures are very hydrophobic, being 2/3 non-polar and having more than 1/2 the polar part formed by groups that H-bond within their own piece of secondary structure or which are partially accessible to the solvent. As the 6 proteins increase in MW they bury an increasing proportion of their non-polar surface (60-79%) and a constant proportion of their polar surface (75%). The implications of these results for the theory of protein structure are discussed. An appendix shows that the accessible surface area of folded proteins is simply proportional to the 2/3 power of their molecular weight.