SsIGPS_reaction_coordinates.png
Summary
Description SsIGPS reaction coordinates.png | 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 | ||
Permission
( Reusing this file ) |
I, the copyright holder of this work, hereby publish it under the following licenses:
This file is licensed under the
Creative Commons
Attribution-Share Alike
Attribution-Share Alike 4.0 International
,
3.0 Unported
,
2.5 Generic
,
2.0 Generic
and
1.0 Generic
license.
You may select the license of your choice.
|