Caching of a chameleon segment facilitates folding of a protein with end-to-end β-sheet
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.
Journal of Physical Chemistry B
Caching of a chameleon segment facilitates folding of a protein with end-to-end β-sheet.
Journal of Physical Chemistry B,
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