Energy minimization method using automata network for sequence and side-chain conformation prediction from given backbone geometry.
Globular proteins have high packing densities as a result of residue side chains in the core achieving a tight, complementary packing. The internal packing is considered the main determinant of native protein structure. From that point of view, we present here a method of energy minimization using an automata network to predict a set of amino acid sequences and their side-chain conformations from a desired backbone geometry for de novo design of proteins. Using discrete side-chain conformations, that is, rotamers, the sequence generation problem from a given backbone geometry becomes one of combinatorial problems. We focused on the residues composing the interior core region and predicted a set of amino acid sequences and their side-chain conformations only from a given backbone geometry. The kinds of residues were restricted to six hydrophobic amino acids (Ala, Ile, Met, Leu, Phe, and Val) because the core regions are almost always composed of hydrophobic residues. The obtained sequences were well packed as was the native sequence. The method can be used for automated sequence generation in the de novo design of proteins.
Kono
H
H
Department of Biotechnology, University of Tokyo, Japan.
Doi
J
J
D001426:Bacterial Proteins; D003198:Computer Simulation; D003573:Cytochrome b Group / Q000737:chemistry; D029968:Escherichia coli Proteins; D008432:Mathematical Computing; D008958:Models, Molecular; D016571:Neural Networks, Computer; D011487:Protein Conformation; D012260:Ribonucleases / Q000737:chemistry; D014305:Triose-Phosphate Isomerase / Q000737:chemistry
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; C017850:cytochrome b562, E coli; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease; D014305:Triose-Phosphate Isomerase