Energy landscape and native-state structure of proteins —A simplified model
International School for Advanced Studies and
V. Beirut 2, Trieste, Italy
2 Department of Physics, 104 Davey Laboratory, The Pennsylvania State University University Park, PA 16802 USA
Accepted: 28 February 2002
We present a theoretical framework for the study of the protein folding problem and apply it to the helix, a β-hairpin structure and to one globular protein. The knowledge of the native-state structure of a protein can be used to deduce the free-energy landscape and to probe the dynamical behavior of proteins.
PACS: 87.15.Aa – Theory and modeling; computer simulation / 64.60.Cn – Order-disorder transformations; statistical mechanics of model systems / 87.10.+e – General theory and mathematical aspects
© EDP Sciences, 2002