Thermodynamic Characterization of 5′-AMP Binding to Bovine Liver Glycogen Phosphorylase a

Abstract

The binding of adenosine 5-monophosphate to liver glycogen phosphorylase a (EC 2.4.1.1) has been studied by size exclusion high performance liquid chromatography and isothermal titration microcalorimetry at pH 6.

Enthalpy of captopril‐angiotensin I‐converting enzyme binding

“…The binding process is accompanied by a large positive entropy change, which depends also strongly on temperature, while Δ G ° changes little with temperature because of the enthalpy‐entropy compensation. This behavior has been found in many ligand‐protein interactions [23, 24, 30, 39–41].…”

“…3 . A rather high negative Δ C p value is normal in binding studies [24, 30, 34, 35], and is a distinctive feature of site‐specific binding [36–38].…”

“…A circulating water bath was used to help stabilize the experimental temperature. The titration experiments were carried out as described elsewhere [23, 24]. The instrument was calibrated by (i) measuring the area under a test electrical heat pulse and comparing it with the heat input and (ii) measuring the heat of a standard chemical reaction.…”

Immobilization of arginase and its application in an enzymatic chromatographic column: Thermodynamic studies of nor-NOHA/arginase binding and role of the reactive histidine residue

“…4). This behaviour has been found in many ligand-protein interactions [61][62][63][64][65][66]. At low temperature, below ≈15 • C, the positive enthalpy change and positive entropy change of binding upon complex formation can be justified by charge-charge interactions and hydrophobic forces [67,68].…”

Thermodynamic Description of the Effect of the Mutation Y49F on Human Glutathione Transferase P1-1 in Binding with Glutathione and the Inhibitor S-Hexylglutathione

“…6, a linear dependence of ⌬H with the temperature was observed, from the slope of which the change in heat capacity (⌬C p ) upon the binding of ligand was obtained (Table IV). A plot of ⌬H versus T⌬S 0 values for the binding of GSH at different temperatures shows a slope near unity (data not shown), which is common for protein-ligand binding processes (21,29,30) and antibody-antigen recognition (31, 32), and has been described in terms of enthalpy/entropy compensation. This is a direct consequence of a large ⌬C p value, since (Ѩ⌬H/ѨT) p ϭ ⌬C p and (Ѩ(T⌬S)/ѨT) p ϭ ⌬C p ϩ ⌬S, and then if ⌬C p Ͼ Ͼ ⌬S , the changes in ⌬H and T⌬S with temperature will be roughly the same (ϭ ⌬C p ) and will compensate each other.…”