文章基本信息

标题：Role of subunit interfaces in the allosteric mechanism of hemoglobin
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作者：C Chothia ; S Wodak ; J Janin 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1976
卷号：73
期号：11
页码：3793-3797
DOI：10.1073/pnas.73.11.3793
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.