Flexibly varying folding mechanism of a nearly symmetrical protein: B domain of protein A.

Proceedings of the National Academy of Sciences of the United States of America
Kazuhito Itoh, Masaki Sasai

Abstract

The folding pathway of the B domain of protein A is the pathway most intensively studied by computer simulations. Recent systematic measurement of Phi values by Sato et al., however, has shown that none of the published computational predictions is consistent with the detailed features of the experimentally observed folding mechanism. In this article we use a statistical mechanical model of folding to show that sensitive dependence of multiple transition state ensembles on temperature and the denaturant concentration is the key to resolving the inconsistency among simulations and the experiment. Such sensitivity in multiple transition state ensembles is a natural consequence of symmetry-breaking in a nearly symmetrical protein.

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Citations

Jan 11, 2008·European Biophysics Journal : EBJ·Ylva IvarssonStefano Gianni
Jan 31, 2008·Proceedings of the National Academy of Sciences of the United States of America·Erik D Nelson, Nick V Grishin
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Apr 5, 2011·The Journal of Chemical Physics·Kazuhito Itoh, Masaki Sasai
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