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Hydrophobic patches on protein subunit interfaces: Characteristics and prediction

✍ Scribed by Philip Lijnzaad; Patrick Argos

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 250 KB
Volume: 28
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199707)28:3<333::aid-prot4>3.0.co;2-d

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✦ Synopsis

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.

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