Motokazu KAMIMURA (email@example.com)
Yoshimasa TAKAHASHI (firstname.lastname@example.org)
Laboratory for Molecular Information Systems,
Department of Knowledge-based Information Engineering,
Toyohashi University of Technology, Toyohashi, Aichi 441 JAPAN
This paper describes the discrimination of phi-psi conformational pattern classes for protein amino acid residues which were defined in our previous works. Statistical discriminant analysis technique has been employed for the present analysis. Each residue was characterized by its peripheral physicochemical environment. The environment was described in a vector representation of which components involve Van der Waals volume, hydrophobic parameter pi, and partial charges of a carbon atom, hydrogen atom of NH and oxygen atom of C'O of ten neighbor residues (five neighbors in each terminal side of the target residue). The discriminant functions obtained with 67 proteins taken from the PDB file correctly discriminated 58.3% of the residues for their conformational pattern classes.