SsIGPS_reaction_coordinates.png


Summary

Description The reaction coordinate diagram for SsIGPS at pH 7.8 and 25°C. The refolding reaction begins in the unfolded, U state, initially misfolds to the I BP intermediate state, partially unfolds to reach the I A intermediate state whose conversion to the subsequent I B intermediate state is rate-limiting. The final step is the conversion of I B to the native state, N. The I A and I B kinetic intermediates correspond to the intermediate observed in equilibrium unfolding studies. The ordinate represents the free energy of each state in the folding reaction mechanism in kcal mol -1 . The abscissa represents the dependence of the difference in free energy between 2 states on the denaturant concentration and is proportional to the change in buried surface, referenced to the U state. The kinetic folding mechanism, illustrating the flow of the unfolded protein to the native conformation is shown beneath the reaction coordinate diagram.
Date 5/2/2020
Source Author supplied
Author Deepesh Nagarajan
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