Premium
Structure optimization of an artificial neural filter detecting membrane‐spanning amino acid sequences
Author(s) -
Lohmann Reinhard,
Schneider Gisbert,
Wrede Paul
Publication year - 1996
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199601)38:1<13::aid-bip2>3.0.co;2-z
Subject(s) - chemistry , artificial neural network , amino acid , membrane , membrane filter , artificial intelligence , filter (signal processing) , biological system , biochemistry , computer science , computer vision , biology
An artificial neural network has been developed for the recognition and prediction of transmembrane regions in the amino acid sequences of human integral membrane proteins. It provides an additional prediction method besides the common hydrophobicity analysis by statistical means. Membrane/nonmembrane transition regions are predicted with 92% accuracy in both training and independent test data. The method used for the development of the neural filter is the algorithm of structure evolution. It subjects both the architecture and parameters of the system to a systematical optimization process and carries out local search in the respective structure and parameter spaces. The training technique of incomplete induction as part of the structure evolution provides for a comparatively general solution of the problem that is described by input‐output relations only. Seven physicochemical side‐chain properties were used to encode the amino acid sequences. It was found that geometric parameters like side‐chain volume, bulkiness, or surface area are of minor importance. The properties polarity, refractivity, and hydrophobicity, however, turned out to support feature extraction. It is concluded that membrane transition regions in proteins are encoded in sequences as a characteristic feature based on the respective side‐chain properties. The method of structure evolution is described in detail for this particular application and suggestions for further development of amino acid sequence filters are made. © 1996 John Wiley & Sons, Inc.