Far UV CD, relative activity and thermal unfolding of the proteins.

<p>(A) Far UV CD scans between 190–260 nm of the type-1, -type2 and mutant LinA proteins show that the mutants are well-folded comparable to the corresponding native proteins (B) The relative activity (%) is shown plotted against time (min). The mutants correspond to those detailed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050373#pone-0050373-t003" target="_blank">Table3</a>. Residual α-HCH dehydrochlorinase activity was measured after pre-incubation of LinA proteins at 60°C for different time periods. Activities prior to pre-incubation were taken as 100%. (C) Thermal unfolding of the proteins followed by Circular dichroism spectroscopy. Clearly mutants that contain Q20 and G23 exhibit higher thermostability comparable to that of the native -type2 protein.