Isothermal titration calorimetry (ITC) is a technique that is capable of quantifying the
stoichiometry, equilibrium constants and thermodynamics of molecular binding events. Thus …

The thermodynamics of metals ions binding to proteins and other biological molecules can
be measured with isothermal titration calorimetry (ITC), which quantifies the binding …

ITC measurements involving metal ions are susceptible to a number of competing reactions
(oxidation, precipitation, and hydrolysis) and coupled reactions involving the buffer and …

Background The binding of metal ions to proteins is a crucial process required for their
catalytic activity, structural stability and/or functional regulation. Isothermal titration …

The binding of Ni (II) and Cu (II) to histidine, to the tripeptides GlyGlyHis and HisGlyHis, and
to the protein bovine serum albumin has been studied by isothermal titration calorimetry …

Determination of binding parameters for metal ion binding to proteins usually requires
preceding steps to remove protein-bound metal ions. Removal of bound metal ions from …

Background ITC is a powerful technique that can reliably assess the thermodynamic
underpinnings of a wide range of binding events. When metal ions are involved …

Protein-protein interactions play important roles for a variety of cell functions, often involving
metal ions; in fact, metal-ion binding mediates and regulates the activity of a wide range of …

Isothermal titration calorimetry is a widely used biophysical technique for studying the
formation or dissociation of molecular complexes. Over the last 5 years, much work has …

Metal ions play many critical roles in biology, as structural and catalytic cofactors, and as cell
regulatory and signalling elements. The metal–protein affinity, expressed conveniently by …