Chothia C, Janin J
Nature. 1975 Aug 28;256(5520):705-8. doi: 10.1038/256705a0.
The formation of the protein-protein interface by the insulin dimer, the trypsin-PTI complex and the alphabeta oxyhaemoglobin dimer removes 1,130-1,720 A2 of 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 complementarily plays a selective role in deciding which proteins may associate.
胰岛素二聚体、胰蛋白酶 - 蛋白酶抑制剂复合物以及αβ 氧合血红蛋白二聚体形成蛋白质 - 蛋白质界面时，会使1130 - 1720 Ų 的可及表面不再与水接触。形成界面的残基紧密堆积：每个残基在氨基酸晶体中占据的体积相同。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方面起选择性作用。
