Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

We apply the Wako-Saito-Muñoz-Eaton model to the study of myotrophin, a small ankyrin repeat protein, whose folding equilibrium and kinetics have been recently characterized experimentally. The model, which is a native-centric with binary variables, provides a finer microscopic detail than the Ising model that has been recently applied to some different repeat proteins, while being still amenable for an exact solution. In partial agreement with the experiments, our results reveal a weakly three-state equilibrium and a two-state-like kinetics of the wild-type protein despite the presence of a nontrivial free-energy profile. These features appear to be related to a careful "design" of the free-energy landscape, so that mutations can alter this picture, stabilizing some intermediates and changing the position of the rate-limiting step. Also, the experimental findings of two alternative pathways, an N-terminal and a C-terminal one, are qualitatively confirmed, even if the variations in the rates upon the experimental mutations cannot be quantitatively reproduced. Interestingly, the folding and unfolding pathways appear to be different, even if closely related: a property that is not generally considered in the phenomenological interpretation of the experimental data.

Citation

Mauro Faccin, Pierpaolo Bruscolini, Alessandro Pelizzola. Analysis of the equilibrium and kinetics of the ankyrin repeat protein myotrophin. The Journal of chemical physics. 2011 Feb 21;134(7):075102

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 21341874

View Full Text