Structure Of Mcfabz Protein

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concentration of inhibitors have been shown in Figure 8A-8F. Overall all the inhibitors binding leads to changes in tertiary structure of McFabZ protein as evident from figure. Increase in the ligand concentration leads to changes in near-UV spectra arises of all three aromatic amino acids (Phe, Tyr and Trp). BiochaninA and Genistein binding have produced similar kind of effect on near-UV spectra. Daidzein has affected more Phe (255nm -270 nm) and Tyr regions (275 nm-282 nm). Catechin gallate has shown more effects in phe and trp (290 nm-305 nm) regions. Altogether we can say that regular decrease in MRE at 280nm is observed upon inhibitors binding. Alternations in MRE towards more negative value corresponds to more flexibility of…show more content…
λmax emission shifted to 343 nm, 349 nm and 348 nm as shown in Figure 9A. Biochanin A and Genistein showed similar kind of effect on McFabZ fluorescence. In both cases fluorescence intensity decreased when compared to native spectra while red shift is observed in λmax emission (Figure 9B & 9C). In case of juglone and daidzein blue shift is observed (Figure 9D &9E). Overall we can say that ligand binding to McFabZ protein leads to decrease in fluorescence intensity. 3.6 Thermodynamic analysis of binding of inhibitors to McFabZ
The binding of McFabZ protein with different inhibitors was studied using Isothermal Titration Calorimetry (ITC). The compounds used for titration against McFabZ were genistein, biochanin A, daidzein, juglone, myricetin and quercetin. ITC data obtained was solved using one site model analysis program of Origin7. Thermodynamic parameters - Enthalpy change (ΔH), Entropy change (ΔS), Gibbs free energy (ΔG) and Equilibrium dissociation constant (KD) have been calculated. Table 3 shows the thermodynamic parameters of binding. Α clear 1:1 stoichiometric binding was observed in all cases except myricetin (N= 1.90 ± 0.293). Downward trend in the ITC profile (Figure 10) reveals an exothermic profile of reaction while upward trend corresponds to the endothermic nature of reaction. ITC titration data describing the binding of biochanin A (A), daidzein

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