Abstract
The formation of the protein–protein interface by the insulin dimer, the trypsin-PTI complex and the αβ oxyhaemoghbin dimer removes 1,130–1,720 Å2 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 complementarity plays a selective role in deciding which proteins may associate.
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Chothia, C., Janin, J. Principles of protein–protein recognition. Nature 256, 705–708 (1975). https://doi.org/10.1038/256705a0
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DOI: https://doi.org/10.1038/256705a0
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