(1) The positive correlations lend support to the claim that a coupling free energy may reflect a state in which enthalpy and entropy components compensate for each other.(2) So, we can get useful work out of a system by reducing enthalpy or by increasing entropy (increasing the amount of disorder).(3) First, the volume change and the enthalpy change of the protein can be determined in time domain without temperature variation or solvent variation method.(4) In addition, melting requires significant amounts of extra heat, (in thermodynamic terms, the enthalpy of fusion), to break molecular bonds and cause a phase transition from solid to liquid.(5) The enthalpy , entropy, and free energy changes in the opening reaction of each basepair are determined from the temperature dependence of the exchange rates.(6) The internal energy of a system, like the enthalpy , is a state property, so it is fixed when the state of the system is specified.(7) Thermogram transition temperatures, enthalpies , and widths at half-height were determined using the software provided with the calorimeter.(8) Unlike enthalpies , component entropies are nonadditive.(9) We have modeled the closing kinetics and in so doing have obtained stacking enthalpies and entropies for single-stranded nucleic acids.(10) Scanning calorimetry is used as a direct method to reveal the thermodynamic properties of phase transition like transition temperatures and enthalpies .
