title: Assessment of pseudo-energy potentials by the best-five test: a new use of the three-dimensional profiles of proteins.
abstract: We propose a new assessment, called the best-five test, for the pseudo-energy potential empirically derived from the protein structural database. The object of the test is the three-dimensional (3D) profiles of proteins, which are directly connected to the pseudo-energy potentials. In the 3D profile, the fitness of each amino acid type is ranked at each residue site of a protein. A site whose native residue type is ranked within the best-five out of 20 amino acids is regarded as satisfactory and the ratio of the satisfactory sites over all the sites of all the proteins examined is indicative of the efficiency of the pseudo-energy potential employed. We applied the test to our potential function consisting of four terms; side-chain packing, hydration, backbone hydrogen-bonding and local conformation, by setting various kinds of definitions for each term. Through this test, the validity of the minus average operation is confirmed, where the energy level of potential functions is adjusted by referring to the random-environmental state of the proteins. Especially in the side-chain packing function, the success ratio increases from about 30 to 50% with this operation. Failure without the operation is ascribed to bulky hydrophobic residues, which almost always occupy higher ranking positions in the 3D profile table. A maximum success ratio of 55.6% was attained with the final potential set consisting of the above four terms. The efficiency of the final set was further checked in the fold-recognition test for distantly related proteins. The best-five test is a new use of the 3D profile table for assessing the ability of the pseudo-energy potentials.
authors.affiliation: National Institute of Genetics, Shizuoka, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Ota
authors.forename: K
authors.initials: K
authors.lastname: Nishikawa
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008969:Molecular Sequence Data; D008995:Monoamine Oxidase / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D008995:Monoamine Oxidase