Principles of protein-protein recognition.
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.
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003201:Computers; D006860:Hydrogen Bonding; D007328:Insulin; D010108:Oxyhemoglobins; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins; D012997:Solvents; D013329:Structure-Activity Relationship; D013499:Surface Properties; D013816:Thermodynamics; D014357:Trypsin / Q000378:metabolism; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000378:metabolism; D014867:Water
D007328:Insulin; D010108:Oxyhemoglobins; D011506:Proteins; D012997:Solvents; D014867:Water; D014359:Trypsin Inhibitor, Kazal Pancreatic; D014357:Trypsin