HYDROPHOBIC PATCHES ON PROTEIN SUBUNIT INTERFACES - CHARACTERISTICS AND PREDICTION

Citation
P. Lijnzaad et P. Argos, HYDROPHOBIC PATCHES ON PROTEIN SUBUNIT INTERFACES - CHARACTERISTICS AND PREDICTION, Proteins, 28(3), 1997, pp. 333-343
Citations number
14
Categorie Soggetti
Biology
Journal title
ISSN journal
08873585
Volume
28
Issue
3
Year of publication
1997
Pages
333 - 343
Database
ISI
SICI code
0887-3585(1997)28:3<333:HPOPSI>2.0.ZU;2-D
Abstract
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.