Topological properties of the energy landscape of small peptides.
In several works it has been shown that the interplay between short range and long range interactions, mimicking the hydrophobic effect, leads to the formation of the typical secondary structures in proteins, alpha-helices and beta-sheets. In this work we study in detail how the general properties of the energy landscape emerge in a model that presents both components. In this regard it proves useful a sort of perturbative approach. In our model many features of the energy landscape in absence of long range interaction can be determined analytically. The comparison between the energy landscape of this reduced model to that of the complete model gives interesting insight on the role of long range interactions.
Bongini
Lorenzo
L
Cell and Molecular Biology Department, Karolinska Institute, P.O. Box 285, SE-171 77 Stockholm, Sweden.
Rampioni
Aldo
A
D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
D010455:Peptides