title: Engineering of stable and fast-folding sequences of model proteins.
abstract: The statistical mechanics of protein folding implies that the best-folding proteins are those that have the native conformation as a pronounced energy minimum. We show that this can be obtained by proper selection of protein sequences and suggest a simple practical way to find these sequences. The statistical mechanics of these proteins with optimized native structure is discussed. These concepts are tested with a simple lattice model of a protein with full enumeration of compact conformations. Selected sequences are shown to have a native state that is very stable and kinetically accessible.
authors.affiliation: Department of Chemistry, Harvard University, Cambridge, MA 02138.
authors.forename: E I
authors.initials: EI
authors.lastname: Shakhnovich
authors.forename: A M
authors.initials: AM
authors.lastname: Gutin
mesh_terms: D007700:Kinetics; D008962:Models, Theoretical; D011487:Protein Conformation; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D011506:Proteins