Caching of a chameleon segment facilitates folding of a protein with end-to-end β-sheet
Document Type
Article
Publication Date
11-27-2008
Abstract
We report results from all-atom simulations of a 49-residue C-terminal fragment of TOP7 in implicit solvent. Using parallel tempering simulations with high statistics, we probe the thermodynamic properties of the protein over a large range of temperatures and evaluate its free energy landscape at room temperature. Our results confirm that the protein folds by a caching mechanism that relies on a chameleon segment. This mechanism differs from the one seen in high-temperature unfolding simulations. Finally, we discuss a possible mechanism for dimerization of the protein. © 2008 American Chemical Society.
Publication Title
Journal of Physical Chemistry B
Recommended Citation
Mohanty, S.,
&
Hansmann, U.
(2008).
Caching of a chameleon segment facilitates folding of a protein with end-to-end β-sheet.
Journal of Physical Chemistry B,
112(47), 15134-15139.
http://doi.org/10.1021/jp804661t
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/8125