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. Author manuscript; available in PMC: 2012 Dec 4.
Published in final edited form as: Biochim Biophys Acta. 2010 Jul 21;1804(11):2136–2145. doi: 10.1016/j.bbapap.2010.07.013

Table 1.

Thermodynamic parameters derived from urea-mediated unfolding studies of catalase-peroxidase from Magnaporthe grisea (MagKatG1) and Synechocystis PCC6803 (SynKatG).

Methods ΔG°H2O
(kJ mol−1)
 m
(kJ mol−1 M−1)
 Cm
(M)
MagKatG1 SynKatG MagKatG1 SynKatG MagKatG1 SynKatG
UV–vis 6.4 9.6 3.2 6.5 2.0 1.5
[θ]412 6.2 10.5 4.9 7.2 1.3 1.5
Trp fluorescence. N-terminal domain n.c. 3.1 n.c. 6.8 n.c. 0.5
Trp fluorescence. C-terminal domain 6.5 6.3 2.3 2.6 2.8 2.4

ΔG°H2O, conformational stabilitye34; m, efficacy of urea in unfolding; Cm, urea concentration with K=[U]/[N]=1. n.c., could not be calculated from experimental data.