Journal: bioRxiv

Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

doi: 10.64898/2026.01.05.697744

Figure Lengend Snippet: ITC traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.

Article Snippet: Binding constants were determined by fitting the change in enthalpy to a single site binding model using MicroCal ITC Origin analysis software.

Techniques: Injection, Binding Assay

Journal: Nucleic Acids Research

Article Title: Molecular determinants for recognition of serotonylated chromatin

doi: 10.1093/nar/gkaf612

Figure Lengend Snippet: H3Q5ser stabilizes Taf3-PHD/H3K4me2 and Taf3-PHD/H3K4me3 complexes. ( A ) Experimental (blue) and fitted (red) spectra of free, ∼50% bound, and fully bound TAF3-PHD resonances E862 and C896 for H3K4me3/H3K4me3Q5ser complex. Transfer peaks indicated with *. Experimental spectrum of E862 is also shown separately for clarity. ( B ) ITC analysis of GST-tagged Taf3-PHD binding to H3K4me3 in yellow and H3K4me3Q5ser in navy blue. Top panel displays the raw heat change per injection of H3 peptide. Bottom panel represents the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software.

Article Snippet: ITC data were subsequently analysed and fitted with the one-site binding model in the MicroCal ITC Origin Analysis software 7.0 (Table , Figs and , , and ).

Techniques: Binding Assay, Injection, Software

Journal: Nucleic Acids Research

Article Title: Molecular determinants for recognition of serotonylated chromatin

doi: 10.1093/nar/gkaf612

Figure Lengend Snippet: Taf3-PHD P881 and W894 form key interaction surface with the serotonin group. ( A ) ITC analysis of GST-tagged Taf3-PHD mutants, BPTF-PHD , PHF2-PHD, or PHF8-PHD with the peptides H3K4me3 (in yellow) and H3K4me3Q5ser (in blue). Top panels display the raw heat change per injection of H3 peptide. Bottom panels represent the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software. ( B ) Multiple sequence alignment (MSA) of human PHD fingers for which high-resolution structures in complex with H3K4me3 are available (ASH1L PDB: 8VLF; BPTF(2) PDB: 2FUU; DIDO1 PDB: 4L7X; ING1 PDB: 2QIC; ING4 PDB: 2PNX/2VNF; ING5 PDB: 3C6W; KMT2E PDB: 4L58; PHF2 PDB: 3KQI; PHF13 PDB: 3O7A; UHRF1 PDB: 3SOW). Consensus Cys4–His–Cys3 positions are highlighted in grey and indicated on top. Locations of the secondary structure elements of TAF3-PHD are indicated on top. S880 and A902 are highlighted in purple, while P881 and W894 are highlighted in yellow.

Article Snippet: ITC data were subsequently analysed and fitted with the one-site binding model in the MicroCal ITC Origin Analysis software 7.0 (Table , Figs and , , and ).

Techniques: Injection, Binding Assay, Software, Sequencing