Rapid measurement of binding constants and heats of binding using a new titration calorimeter.

By T. Wiseman, Samuel H. Williston, J. Brandts, Lung-Nan Lin. 1989

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Citations in the corpus

Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, methodology): “0) via a PD-10 column (Cytiva Life Sciences), and the titration calorimetry measurements were performed using a Malvern MicroCAL ITC calorimeter as previously described (89).”
SEDPHAT – a platform for global ITC analysis and global multi-method analysis of molecular interactions (2014, background): “Unique among biophysical techniques, it observes directly the heat change ΔQ of a solution associated with a change of composition {Δci} during the titration of a macromolecular component in the cell with increasing amounts of its binding partner(s) [2,3].”
Best Practices for Constructing, Preparing, and Evaluating Protein-Ligand Binding Affinity Benchmarks [Article v1.0] (2021, background): “In addition, ITC data are often only available for a narrow dynamic range [109, 110].”
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. (2000, methodology): “The position Binding of protein fragments and peptides to the TPR domains was measured by isothermal titration calorimetry (Wiseman et al., 1989) of one nickel atom was determined by analysis of an anomalous”
Best practices for constructing, preparing, and evaluating protein-ligand binding aﬃnity benchmarks [Article v0.2] (2021, background): “In addition, ITC data are often only available for a narrow dynamic range [109, 110].”