Principles of protein-protein recognition. Export

@article{chothia:75, abstract = {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.}, author = {Chothia, C. and Janin, J.}, citeulike-article-id = {3863679}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/1153006}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=1153006}, day = {28}, issn = {0028-0836}, journal = {Nature}, keywords = {interactions, protein-protein}, month = {August}, number = {5520}, pages = {705--708}, posted-at = {2009-01-08 21:01:49}, priority = {0}, title = {Principles of protein-protein recognition.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/1153006}, volume = {256}, year = {1975} }

TY - JOUR ID - chothia:75 L3 - citeulike-article-id:3863679 N2 - 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. IS - 5520 JF - Nature SN - 0028-0836 EP - 708 TI - Principles of protein-protein recognition. VL - 256 SP - 705 KW - interactions KW - protein-protein AU - Chothia, C AU - Janin, J PY - 1975/08/28/ UR - http://view.ncbi.nlm.nih.gov/pubmed/1153006 ER -