Folding of proteins with diverse folds
Document Type
Article
Publication Date
1-1-2006
Abstract
Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our energy function find the native structures as global minima in free energy at experimentally relevant temperatures. However, the folding process strongly differs for the three molecules, indicating that the folding mechanism is correlated with the form of the native structure. © 2006 by the Biophysical Society.
Publication Title
Biophysical Journal
Recommended Citation
Mohanty, S.,
&
Hansmann, U.
(2006).
Folding of proteins with diverse folds.
Biophysical Journal,
91(10), 3573-3578.
http://doi.org/10.1529/biophysj.106.087668
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/13515