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SsIGPS_reaction_coordinates.png (372 × 340 pixels, file size: 21 KB, MIME type: image/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 IBP intermediate state, partially unfolds to reach the IA intermediate state whose conversion to the subsequent IB intermediate state is rate-limiting. The final step is the conversion of IB to the native state, N. The IA and IB 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
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Author Deepesh Nagarajan
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current10:13, 5 February 2020Thumbnail for version as of 10:13, 5 February 2020372 × 340 (21 KB)Evolution and evolvability{{Information |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 IBP intermediate state, partially unfolds to reach the IA intermediate state whose conversion to the subsequent IB intermediate state is rate-limiting. The final step is the conversion of IB to the native state, N. TheIA and IB kinetic intermediates correspond to the intermediate observed in equilibrium unfolding studies. T...

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