Table 1 Conformational stability parameters of the native and mutant MtbICL.

From: Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility

Protein

Urea

GdnHCl

C m [M]

ΔGH20 (cal.mol−1)

C m [M]

ΔGH20 (cal.mol−1)

MtbICL

3.9

1432.9 ± 76.7

2.1

1335.3 ± 79.5

MtbICLF345A

2.9

1070.4 ± 64.2

1.5

879.9 ± 38.4

  1. Unfolding studies were done at various concentrations of urea and GdnHCl as described in the Experimental section. The C m and ΔGH20 values are based on three independent experiments for each measurement and mean ± SD was taken.
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