Hydrophobic patches, defined as clusters of neighboring apolar atoms d
eemed accessible on a given protein surface, have been investigated on
protein subunit interfaces. The data were taken from known tertiary s
tructures of multimeric protein complexes. Amino acid composition and
preference, patch size distribution, and patch contact complementarity
across associating subunits were examined and compared with hydrophob
ic patches found on the solvent-accessible surface of the multimeric c
omplexes, The largest or second largest patch on the accessible surfac
e of the entire subunit was involved in multimeric interfaces in 90% o
f the cases. These results should prove useful for subunit design and
engineering as well as for prediction of subunit interface regions. (C
) 1997 Wiley-Liss, Inc.