title: Beta-sheet preferences from first principles.
abstract: The natural amino acids have different preferences of occurring in specific types of secondary protein structure. Simulations are performed on periodic model beta-sheets of 14 different amino acids, at the level of density functional theory, employing the generalized gradient approximation. We find that the statistically observed beta-sheet propensities correlate very well with the calculated binding energies. Analysis of the calculations shows that the beta-sheet propensities are determined by the local flexibility of the individual polypeptide strands.
authors.affiliation: Center for Atomic-scale Materials Physics, Technical University of Denmark, DK-2800 Lyngby, Denmark.
authors.forename: Jan
authors.initials: J
authors.lastname: Rossmeisl
authors.forename: Iben
authors.initials: I
authors.lastname: Kristensen
authors.forename: Misha
authors.initials: M
authors.lastname: Gregersen
authors.forename: Karsten W
authors.initials: KW
authors.lastname: Jacobsen
authors.forename: Jens K
authors.initials: JK
authors.lastname: Nørskov
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D003198:Computer Simulation; D008956:Models, Chemical; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D011506:Proteins