A method for the detection of hydrophobic patches on the surfaces of p
rotein tertiary structures is presented, it delineates explicit contig
uous pieces of surface of arbitrary size and shape that consist solely
of carbon and sulphur atoms using a dot representation of the solvent
-accessible surface, The technique is also useful in detecting surface
segments with other characteristics, such as polar patches, Its poten
tial as a tool in the study of protein-protein interactions and substr
ate recognition is demonstrated by applying the method to myoglobin, L
eu/Ile/Val-bonding protein, lipase, lysozyme, azurin, triose phosphate
isomerase, carbonic anhydrase, and phosphoglycerate kinase. Only the
largest patches, having sizes exceeding random expectation, are deemed
meaningful, in addition to well-known hydrophobic patches on these pr
oteins, a number of other patches are found, and their significance is
discussed, The method is simple, fast, and robust. The program text i
s obtainable by anonymous ftp. (C) 1996 Wiley-Liss, Inc.