title: Gauss-function-Based model of hydrophobicity density in proteins.
abstract: The model adopting the three-dimensional Gauss function to express the hydrophobicity distribution in proteins is presented in this paper. The tendency to create the hydrophobic center during protein folding is expressed in form of an external force field of the form of three-dimensional Gauss function which directs the folding polypeptide to locate the hydrophobic residues in a central part of the molecule and hydrophilic ones exposed toward the molecular surface. The decrease of the differences between hydrophobicity distribution as it appears at each step of the folding simulation and the expected hydrophobicity distribution (three-dimensional Gauss function) is the convergence criterion together with traditional non-bonding interaction optimization. The model was applied to fold the hypothetical membrane protein (target protein in CASP6) TA0354_69_121 from Thermoplasma acidophilum.
authors.affiliation: Institute of Biochemistry, Collegium Medicum, Jagiellonian University, Kopernika 7, 31-034 Cracow, Poland. mbkoniec@cyf-kr.edu.pl
authors.forename: Leszek
authors.initials: L
authors.lastname: Konieczny
authors.forename: Michal
authors.initials: M
authors.lastname: Brylinski
authors.forename: Irena
authors.initials: I
authors.lastname: Roterman
mesh_terms: D003198:Computer Simulation; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D016011:Normal Distribution; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013822:Thermoplasma / Q000737:chemistry
chemical_list: D008565:Membrane Proteins; D011506:Proteins