Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase

Conclusions:
The slow temperature-induced unfolding of yeast TIM shows three kinetic phases. Rather than a simple sequential pathway, a complex mechanism involving off-pathway intermediates or even parallel pathways may be operating. β-strand-type residual structure, which appears below pH 8.0, is likely to be associated with increased irreversible aggregation of the unfolded protein. However, this denatured form apparently accelerates the refolding process.

Source: BMC Biochemistry - September 3, 2015 Category: Biochemistry Authors: Ariana Labastida-PolitoGeorgina Garza-RamosMenandro Camarillo-CadenaRafael ZubillagaAndrés Hernández-Arana Source Type: research