title: On the design and analysis of protein folding potentials.
abstract: Pairwise interaction models to recognize native folds are designed and analyzed. Different sets of parameters are considered but the focus was on 20 x 20 contact matrices. Simultaneous solution of inequalities and minimization of the variance of the energy find matrices that recognize exactly the native folds of 572 sequences and structures from the protein data bank (PDB). The set includes many homologous pairs, which present a difficult recognition problem. Significant recognition ability is recovered with a small number of parameters (e.g., the H/P model). However, full recognition requires a complete set of amino acids. In addition to structures from the PDB, a folding program (MONSSTER) was used to generate decoy structures for 75 proteins. It is impossible to recognize all the native structures of the extended set by contact potentials. We therefore searched for a new functional form. An energy function U, which is based on a sum of general pairwise interactions limited to a resolution of 1 angstrom, is considered. This set was infeasible too. We therefore conjecture that it is not possible to find a folding potential, resolved to 1 angstrom, which is a sum of pair interactions.
authors.affiliation: Department of Biological Chemistry, The Hebrew University, Givat Ram, Jerusalem, Israel.
authors.forename: D
authors.initials: D
authors.lastname: Tobi
authors.forename: G
authors.initials: G
authors.lastname: Shafran
authors.forename: N
authors.initials: N
authors.lastname: Linial
authors.forename: R
authors.initials: R
authors.lastname: Elber
mesh_terms: D000465:Algorithms; D000596:Amino Acids / Q000737:chemistry; D016208:Databases, Factual; D008958:Models, Molecular; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012984:Software; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D011506:Proteins