Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7.

ABSTRACT: We present a detailed structural characterization of the intermediate state populated during the folding and unfolding of the bacterial immunity protein Im7. We achieve this result by incorporating a variety of experimental data available for this species in molecular dynamics simulations. First, we define the structure of the exchange-competent intermediate state of Im7 by using equilibrium hydrogen-exchange protection factors. Second, we use this ensemble to predict Phi-values and compare the results with the experimentally determined Phi-values of the kinetic refolding intermediate. Third, we predict chemical-shift measurements and compare them with the measured chemical shifts of a mutational variant of Im7 for which the kinetic folding intermediate is the most stable state populated a

SUBMITTER: Gsponer J 

PROVIDER: S-EPMC1324994 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature