abstract = "An exploration of common rules (property motifs) in
amino acid sequences has been required for the design
of novel sequences and elucidation of the interactions
between molecules controlled by the structural or
physical environment. In the present study, we
developed a new method to search property motifs that
are common in peptide sequence data. Our method
comprises the following two characteristics: (i) the
automatic determination of the position and length of
common property motifs by calculating the
physicochemical similarity of amino acids, and (ii) the
quick and effective exploration of motif candidates
that discriminates the positives and negatives by the
introduction of genetic programming (GP). Our method
was evaluated by two types of model data sets. First,
the intentionally buried property motifs were searched
in the artificially derived peptide data containing
intentionally buried property motifs. As a result, the
expected property motifs were correctly extracted by
our algorithm. Second, the peptide data that interact
with MHC class II molecules were analysed as one of the
models of biologically active peptides with buried
motifs in various lengths. Twofold MHC class II binding
peptides were identified with the rule using our
method, compared to the existing scoring matrix method.
In conclusion, our GP based motif searching approach
enabled to obtain knowledge of functional aspects of
the peptides without any prior knowledge.",
notes = "Department of Biotechnology, School of Engineering,
Nagoya University, Nagoya, Japan.