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Shape complementarity at the hemoglobin α 1 β 1 subunit interface
Author(s) -
Connolly Michael L.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250705
Subject(s) - tetramer , chemistry , dock , complementarity (molecular biology) , protein subunit , dimer , docking (animal) , hemoglobin , trypsin , crystallography , algorithm , biological system , computer science , biochemistry , genetics , gene , biology , nursing , organic chemistry , enzyme , medicine
Abstract A computational method for attempting to predict protein complexes from the coordinates of the individual proteins has been developed. It is based on matching complementary patterns of knobs and holes. The computer algorithm correctly and uniquely predicts the association of the alpha and beta subunits to form the αβ dimer corresponding to the α 1 β 1 interface in the hemoglobin tetramer. It fails to correctly dock trypsin inhibitor onto trypsin. Nevertheless, this lone success is still a significant advance over previous protein‐docking algorithms. The method is also important because it introduces several ways to measure the shape of protein surface regions.