title: Origin of the native driving force for protein folding.
abstract: We derive an expression with four adjustable parameters that reproduces well the 20x20 Miyazawa-Jernigan potential matrix extracted from known protein structures. The numerical values of the parameters can be approximately computed from the surface tension of water, water-screened dipole interactions between residues and water and among residues, and average exposures of residues in folded proteins.
authors.affiliation: Department of Physics and Center for Complex Systems, National Central University, Chung-li, Taiwan 320, Republic of China.
authors.forename: Z H
authors.initials: ZH
authors.lastname: Wang
authors.forename: H C
authors.initials: HC
authors.lastname: Lee
mesh_terms: D004563:Electrochemistry; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013500:Surface Tension
chemical_list: D011506:Proteins