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Standard molar entropy
About: Standard molar entropy is a research topic. Over the lifetime, 1586 publications have been published within this topic receiving 29886 citations.
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TL;DR: In this paper, the authors presented the heat capacity of metastable Li15Si4 as a function of temperature in a range from (2 to 615) K. The measurements were performed using two different calorimeters depending on their specification.
2 citations
01 Jan 1972
TL;DR: It is possible to determine molar entropy values for individual substances, using calculations based on the third law of thermodynamics, which states that the entropy of a pure crystalline substance at 0 K is zero as discussed by the authors.
Abstract: Entropy is a thermodynamic function, which was first defined in engineering thermodynamics regarding the performance of heat engines. The entropy of a system is a measure of the disorder or randomness of the system. Entropy depends only on the state of the system and not on the way in which that state was reached. The entropy of a system is a measure of the disorder or randomness of the system. The value of the entropy change is dependent on the temperature and the pressure. It is possible to determine molar entropy values for individual substances, using calculations based on the third law of thermodynamics, which states that the entropy of a pure crystalline substance at 0 K is zero. Molar entropy values are usually quoted for the substance in its standard state. Standard entropy changes for reactions can be added and subtracted in the same way as heats of reaction, to enable unknown values to be obtained from known values.
2 citations
TL;DR: In this paper, the heat capacity of crystalline Th(NO3)4·5H2O has been determined by adiabatic calorimetry primarily to enable evaluation of the standard partial molar entropy and heat capacity.
2 citations
Journal Article•
TL;DR: In this paper, the binding of nimesulide, a cox-2 inhibitor, to bovine serum albumin was investigated by equilibrium dialysis method at different temperatures and pH conditions.
Abstract: The binding of nimesulide, a cox-2 inhibitor, to bovine serum albumin was investigated by equilibrium dialysis method at different temperatures and pH conditions. The Scatchard plots were prepared based on these drug-protein binding data. The number of binding sites (n), the value of association constant (K) at different conditions and different thermodynamic parameters (i.e., standard free energy change I”G°, standard enthalpy change I”H° and standard entropy change I”S°) of nimesulide-BSA binding were determined. The result shows that number of binding sites is around 2.5 and the value of association constant is decreasing with increasing temperature and pH. It also reveals that the value of I”G° and I”H° were highly negative and I”S° was also negative. The result indicates that the interaction between nimesulide and bovine serum albumin is exothermic and spontaneous in nature. It is postulated that nimesulide-bovine serum albumin interaction may occur due to hydrogen bond formation and ionic interaction.
2 citations
TL;DR: In this paper, the standard molar enthalpy of formation of Cs2Ca[B4O5(OH)4]2·8H2O(s) was derived from the thermodynamic relation with the standard Molar Gibbs free energy of formation, computed from a group contribution method.
2 citations