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Fig. 1 | Epigenetics & Chromatin

Fig. 1

From: MeCP2-E1 isoform is a dynamically expressed, weakly DNA-bound protein with different protein and DNA interactions compared to MeCP2-E2

Fig. 1

Biophysical characterization of the MeCP2-E1 and E2 NTD-MBD domain interaction with DNA. a Schematic representation of the MeCP2-E1 and E2 isoforms depicting the unique NTD amino acid sequences and shared domains. b Fluorescence thermal denaturation curves for E1 and E2 NTD-MBD protein fragments in the presence of unmethylated and mCpG-dsDNA. Unfolding traces were fitted considering a two-state unfolding model. c Unfolding stability parameters obtained from thermal denaturations followed by intrinsic tryptophan fluorescence. d Calorimetric titrations of E1 and E2 NTD-MBD proteins interacting with dsDNA plots show the thermograms (thermal power as a function of time) and the binding isotherms (normalized heats as a function of the dsDNA/protein molar ratio). e Buffer-independent dsDNA binding parameters (Kd, dissociation constant; ΔG: Gibbs free energy of interaction; ΔH: enthalpy of interaction; −TΔS: entropic contribution of interaction; ΔCP: heat capacity of interaction; nH: number of protons exchanged upon complex formation) obtained from calorimetric titrations at pH 7

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