Gluconate is a commonly encountered nutrient, which is degraded by the enzyme gluconokinase to generate 6-phosphogluconate. Here we used isothermal titration calorimetry to study the properties of this reaction. ΔH, KM and kcat are reported along with substrate binding data. We propose that the reaction follows a ternary complex mechanism, with ATP binding first. The reaction is inhibited by gl...

Both enantiomers of trans-cyclohexane-1,2-diammonium sulfate and trans-1,2-diphenylethylenediammonium sulfate were used as "tailor-made" additives to direct the mirror-symmetry breaking in the attrition-enhanced deracemization (i.e. Viedma ripening) of conglomerate crystals of ethylenediammonium sulfate (EDS). Isothermal titration calorimetry (ITC) shows chiral recognition of (1R,2R)- and (1S,2...

Structure-energy relationships for a small group of pyranose and septanose mono-saccharide ligands are developed for binding to Concanavalin A (ConA). The affinity of ConA for methyl "manno"β-septanoside 7 was found to be higher than any of the previously reported mono-septanoside ligands. Isothermal titration calorimetry (ITC) in conjunction with docking simulations and quantum mechanics/molec...

Structural biology now plays a prominent role in addressing questions central to understanding how excitable cells function. Although interest in the insights gained from the definition and dissection of macromolecular anatomy is high, many neurobiologists remain unfamiliar with the methods employed. This primer aims to help neurobiologists understand approaches for probing macromolecular struc...

Doxorubicin (DOX) and Pluronic-PAA interaction was investigated using isothermal titration calorimetry (ITC). DOX/polymer interaction is governed primarily by electrostatic interaction. The uptake of DOX results in the formation of insoluble polymer/DOX complex. Addition of salt weakens the interaction of drug and polymer by charge shielding effect between positive ionized amino group on DOX an...

Isothermal titration calorimetry (ITC) is a popular chemical analysis technique that can be used to measure macromolecular interactions and physical processes. ITC involves the measurement of heat flow from cell after each injection during experiment. has been useful thermodynamics such as protein-ligand or protein-protein binding affinity also processes enzyme catalyzed reactions. The use in b...

All biochemical reactions involve recognition, binding and the formation of noncovalent complexes. Since the characterization of binding events is central to understanding any physiological process at the molecular level, biochemical and biomedical research requires methodologies for precisely analyzing binding reactions. Isothermal titration calorimetry (ITC) is rapidly becoming the method of ...

A thermodynamic study on the interaction of bovine carbonic anhydrase II, CAII, with cobalt(II) and iron(III) ions was made using isothermal titration calorimetry (ITC) at 300.15 K and 310.15 K in Tris buffer solutions at pH = 7.5. The enthalpies of interaction of Co2++ CAII and Fe3++ CAII are reported and analyzed in terms of the extended solvation theory. The results indicate that there are t...

A series of modified saccharin sulfonamides have been designed as carbonic anhydrase (CA) inhibitors and synthesized. Their binding to CA isoforms I, II, VII, XII, and XIII was measured by the fluorescent thermal shift assay (FTSA) and isothermal titration calorimetry (ITC). Saccharin bound the CAs weakly, exhibiting the affinities of 1-10 mM for four CAs except CA I where binding could not be ...