Identification of β-barrel membrane proteins based on amino acid composition properties and predicted secondary structure

Unlike all-helices membrane proteins, beta-barrel membrane proteins can not be successfully discriminated from other proteins, especially from all-beta soluble proteins. This paper performs an analysis on the amino acid composition in membrane parts of 12 beta-barrel membrane proteins versus beta-strands of 79 all-beta soluble proteins. The average and variance of the amino acid composition in these two classes are calculated. Amino acids such as Gly, Asn, Val that are most likely associated with classification are selected based on Fishers discriminant ratio. A linear classifier built with these selected amino acids composition in observed beta-strands achieves 100% classification accuracy for 12 membrane proteins and 79 soluble proteins in a four-fold cross-validation experiment. Since at present the accuracy of secondary structure prediction is quite high, a promising method to identify beta-barrel membrane proteins is presented based on the linear classifier coupled with predicted secondary structure. Applied to 241 beta-barrel membrane proteins and 3855 soluble proteins with various structures, the method achieves 85.48% (206/241) sensitivity and 92.53% specificity (3567/3855). (C) 2002 Elsevier Science Ltd. All rights reserved.