title: Topological properties of the energy landscape of small peptides.
abstract: The topology of the potential energy landscape (PEL) underlying the dynamics of a two dimensional off-lattice model for a heteropolymer is analyzed for different sequences of amino-acids. A statistical characterization of the metastable minima and first-order saddles of the PEL highlights structural differences in the landscape of good and bad folding sequences and provides insight on the chain dynamics during folding.
authors.affiliation: Centro Interdipartimentale per lo Studio delle Dinamiche Complesse, via Sansone, 1-I-50019 Sesto Fiorentino, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Bongini
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding
chemical_list: D010455:Peptides