Topological properties of the energy landscape of small peptides.
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.
Bongini
L
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Centro Interdipartimentale per lo Studio delle Dinamiche Complesse, via Sansone, 1-I-50019 Sesto Fiorentino, Italy.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding
D010455:Peptides