Chothia C, Wodak S, Janin J
Proc Natl Acad Sci U S A. 1976 Nov;73(11):3793-7. doi: 10.1073/pnas.73.11.3793.
We calculate the surface area buried in subunit interfaces of human deoxyhemoglobin and of horse methemoglobin. A larger surface area is buried in deoxy- than in methemoglobin as a result of tertiary and quaternary structure changes. In both molecules the dimer-dimer interface is closepacked. This implies that hydrophobicity stabilizes the deoxystructure, the free energy spent in keeping the subunits in a low-affinity conformation being compensated by hydrophobic free energy due to the smaller surface area accessible to solvent.
我们计算了人类脱氧血红蛋白和马高铁血红蛋白亚基界面中埋藏的表面积。由于三级和四级结构的变化，脱氧血红蛋白中埋藏的表面积比高铁血红蛋白中的更大。在这两种分子中，二聚体 - 二聚体界面都是紧密堆积的。这意味着疏水性稳定了脱氧结构，将亚基保持在低亲和力构象中所消耗的自由能被由于溶剂可及的表面积较小而产生的疏水自由能所补偿。
