Premium
Hydrophobic patches on protein subunit interfaces: Characteristics and prediction
Author(s) -
Lijnzaad Philip,
Argos Patrick
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199707)28:3<333::aid-prot4>3.0.co;2-d
Subject(s) - protein subunit , complementarity (molecular biology) , chemistry , crystallography , biophysics , materials science , biology , biochemistry , genetics , gene
Hydrophobic patches, defined as clusters of neighboring apolar atoms deemed accessible on a given protein surface, have been investigated on protein subunit interfaces. The data were taken from known tertiary structures of multimeric protein complexes. Amino acid composition and preference, patch size distribution, and patch contact complementarity across associating subunits were examined and compared with hydrophobic patches found on the solvent‐accessible surface of the multimeric complexes. The largest or second largest patch on the accessible surface of the entire subunit was involved in multimeric interfaces in 90% of the cases. These results should prove useful for subunit design and engineering as well as for prediction of subunit interface regions. Proteins 28:333–343, 1997. © 1997 Wiley‐Liss, Inc.