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