PRINCIPLES OF PROTEIN-PROTEIN RECOGNITION
PRINCIPLES OF PROTEIN-PROTEIN RECOGNITION
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DOI：
10.1038/256705a0
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发表时间：
1975-01-01
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：
CHOTHIA, C;JANIN, J
胰岛素二聚体、胰蛋白酶-PTI复合物和αβ氧化血红蛋白二聚体形成的蛋白质-蛋白质界面可消除1，130- 1，720 Å 2的可及表面与水的接触。形成界面的残基是紧密堆积的：每个残基占据的体积与氨基酸晶体中的体积相同。这些结果表明，疏水性是稳定蛋白质-蛋白质缔合的主要因素，而互补性在决定哪些蛋白质可能缔合中起选择性作用。
The formation of the protein–protein interface by the insulin dimer, the trypsin-PTI complex and theαβoxyhaemoghbin dimer removes1,130–1,720 Å2of accessible surface from contact with water. The residues forming the interface are close packed: each occupies the same volume as it does in crystals of amino acids. These results indicate that hydrophobicity is the major factor stabilising protein–protein association, while complementarity plays a selective role in deciding which proteins may associate.