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Image Search Results
Journal: eLife
Article Title: Target-agnostic identification of human antibodies to Plasmodium falciparum sexual forms reveals cross stage recognition of glutamate-rich repeats
doi: 10.7554/elife.97865
Figure Lengend Snippet: Figure 4. Binding characteristics of RESA peptides to B1E11K. (A) Various peptides based on the EENV repeat region were designed and conjugated to a biotin-AHX-AHX moiety (AHX = ε-aminocaproic acid). EC50 values obtained from ELISA experiments utilizing various EENV repeat peptides with (B) B1E11K mAb or (C) B1E11K Fab. Error bars represent standard deviation. Biolayer interferometry experiments utilizing immobilized (D) RESA 10AA peptide or (E) RESA P2 (16AA) peptide dipped into B1E11K Fab. Representative isothermal titration calorimetry experiments in which B1E11K Fab was injected into (F) RESA 10AA peptide or (G) RESA P2 (16AA) peptide. (H) Size-exclusion chromatography coupled with multi-angle light scattering (SEC- MALS) of a solution of B1E11K Fab incubated with RESA P2 (16AA) peptide in a 6:1 molar ratio. The predicted molecular weight of the B1E11K Fab and RESA P2 peptide are 46.9 kDa and 2.5 kDa, respectively. The shaded region indicates the fractions collected used for negative-stain electron microscopy (nsEM). (I) An nsEM map reconstruction which permits the fitting of two B1E11K Fabs (Fab A and Fab B).
Article Snippet: The curves were fitted to a 2:1 or 1:1 binding model using the
Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Standard Deviation, Isothermal Titration Calorimetry, Injection, Size-exclusion Chromatography, Multi-Angle Light Scattering, Incubation, Molecular Weight, Staining, Electron Microscopy
Journal: Communications Biology
Article Title: Aromatic patch in whiB-like transcription factors facilitates primary sigma factor interaction in mycobacterium tuberculosis
doi: 10.1038/s42003-026-09698-5
Figure Lengend Snippet: A – C Representative results for Isothermal titration calorimetry (ITC) assay of the interactions between σ A 4 and Mtb Wbls as indicated. The calorimetric titration is shown in the top panel (the raw data in Supplementary DataSet ), with the integrated injection heat derived from the titration and the best-fit curve (dash lines) of a simple 1:1 interaction model shown in the bottom ( D ) Summary of the binding parameters from the best fit, including the association constant ( K a ), dissociation constant ( K d ), changes in enthalpy (ΔH) and entropy (ΔS) upon binding, and the goodness of the fit (Chi /DoF).
Article Snippet: The analysis for the ITC was done using
Techniques: Isothermal Titration Calorimetry, Titration, Injection, Derivative Assay, Binding Assay