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(B) Chain A of Mtb ICL tetramer showing the position of Phe345 in red and active site signature sequence () in green. The active site residues and Phe345 are marked and labeled. There are few reports that show the activity of an enzyme can be lost by a mutation topologically distant from active site.This is usually due to loss of structure and/or stability of the enzyme.Comparative biochemical profiles of native and mutant Mtb ICL. Lowest panel shows chromatogram of known standard molecular weight markers- ferritin (440 k Da at 10.8 m L, in green), catalase (232 k Da at 12.4 m L, in brown), aldolase (158 k Da at 13.2 m L, in blue) and ovalbumin (43 k Da at 15.3 m L, in pink).

To achieve this goal, biochemical experiments and multi-dimensional computational studies were performed on Mtb ICL and Mtb ICL (hereafter referred as native and mutant protein respectively).To obtain a detailed description and understanding of the function of a protein, the 3D structure and an accurate description of its dynamics are therefore required.Proteins interchange between structural states covering a magnitude from 10.The cloned and over-expressed native and mutant proteins were purified as described in the experimental section.The molecular weights of the purified recombinant proteins were determined by SDS-PAGE (Supplementary Fig. On the Superdex 200 column both the proteins showed peak with a retention volume of around 12.6 m L that corresponds to a molecular mass of ~200 k Da (Fig.

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