Understanding the fine balance between changes of entropy and enthalpy and the competition between a guest and water molecules in molecular binding is crucial in fundamental studies and practical applications. Experiments provide measurements. However, illustrating the binding/unbinding processes gives a complete picture of molecular recognition not directly available from experiments, and comp...

The design of specific inhibitors against the Hsp90 chaperone and other enzyme relies on the detailed and correct understanding of both the thermodynamics of inhibitor binding and the structural features of the protein-inhibitor complex. Here we present a detailed thermodynamic study of binding of aryl-dihydroxyphenyl-thiadiazole inhibitor series to recombinant human Hsp90 alpha isozyme. The in...

using uv-vis spectrophotometric method the interaction of water soluble phthalocyanine, cobalt(ιι) 4,4′,4′′,4′′′- tetrasulfophthalocyanine(cotspc), with bovine serum albumin (bsa) to determine the formation constant and related thermodynamic functions. the measurements were considered in 1mm sodium phosphate buffer, ph 7.0 and at 5 different temperatures 20, 25, 30, 35 and 40ºc. the results sho...

The enthalpy change for saturation of half the Fe(II1) binding sites was compared with the enthalpy change for saturation of the hall-saturated protein. In the presence of excess HCOBthese values were -10.90 f 0.19 Cal per mole of bound Fe(II1) and -10.43 f 0.76 Cal per mole of bound Fe(III), respectively. In the absence of HCOI-, corresponding values were -4.64 + 0.05 Cal per mole of bound Fe(...

The interaction of guest molecules ranging from pentan-1-ol to octan-1-ol with α-cyclodextrin (α-CD) in water of has been studied calorimetrically at 283.15, 288.15, 293.15, 298.15 and 308.15 K with an isoperibolic titration calorimeter designed in our laboratory. The calorimetric method employed allows the determination of the thermodynamic parameters characterizing the binding process, ∆G°m, ...

1. The enthalpy changes during individual reaction steps of the myosin subfragment 1 ATPase were studied with the use of a new stopped-flow calorimeter [Howarth, Millar & Gutfreund (1987) Biochem. J. 248, 677-682]. 2. At 5 degrees C and pH 7.0, the endothermic on-enzyme ATP-cleavage step was observed directly (delta H = +64 kJ.mol-1). 3. ADP binding is accompanied by a biphasic enthalpy change....

Alkylammonium binding to DNA was studied by isothermal titration calorimetry. Experimental data, obtained as functions of alkyl chain length, salt concentration, DNA concentration, and temperature, provided a detailed thermodynamic description of lipid-DNA binding reactions leading to DNA condensation. Lipid binding, counterion displacement, and DNA condensation were highly cooperative processe...