Volume 58, Number 4, May 2002
|Page(s)||623 - 629|
|Section||Interdisciplinary physics and related areas of science and technology|
|Published online||01 May 2002|
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
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.