Unwinding the Double Helix: Complete Equation for Chemical Equilibrium

Benzinger, T. H.; Hammer, Caleb F.

doi:10.1016/b978-0-12-152818-8.50034-7

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3 Theories Of Compensation Effect431 Exact Compensation Is I...2

The Planck-benzinger Thermal Work Function: a New State Func1

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Cited by 7 publications

(3 citation statements)

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“…Both parts of entropy are positive definite values, and it can be seen that the compensation entropy does not appear in the free energy G or its changes. The same theory has also been developed by several other authors 43c…”

Section: 3 Theories Of Compensation Effect431 Exact Compensation Is I...mentioning

confidence: 78%

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Isokinetic Relationship, Isoequilibrium Relationship, and Enthalpy−Entropy Compensation

2001

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Section: 3 Theories Of Compensation Effect431 Exact Compensation Is I...mentioning

confidence: 78%

“…In 1971, Benzinger et al . 43a,b showed that the entropy changes in an isothermal, isopiestic process were related through the heat integral in such a way that and …”

Section: 3 Theories Of Compensation Effect431 Exact Compensation Is I...mentioning

confidence: 99%

Isokinetic Relationship, Isoequilibrium Relationship, and Enthalpy−Entropy Compensation

2001

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“…It was Benzinger [22] who recognized that the enthalpy term AHo(T) is a composite term representing both the chemical bonding energy and the heat of a given reaction, such that AHo(T) = AHo(To) + ACpo(T)dT…”

Section: The Planck-benzinger Thermal Work Function: a New State Funcmentioning

confidence: 99%

Approximation of the Planck-Benzinger thermal work function in protein refolding in ribonuclease systems

Chun

1988

Int. J. Quantum Chem.

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In reexamining the thermodynamic parameters of the protein refolding of ribonuclease systems over the temperature range of 220-360" K, based on the Nemst heat theorem, we found that at the temperature (T,), the thennodynamic quantities AGo(T,) and AHo(T,) are of the same magnitude, while TASo(T,) approaches zero. Based on the Planck-Benzinger thermal work function, AWo(T) = AHo(To) -AGo(T). [11] is an effective measure of the ease with which these molecules can be refolded to resemble the native protein structure, with greatest ease of folding at the lowest chemical bond energy. The Planck-Benzinger thermal work function, AWo(T), is an effective measure of the energy potentially available for any interaction to take place. AHo(To), a temperature-invariant quantity, is a primary source of the chemical bond energy essential for any reaction to proceed in a biological system, and is indispensable in any consideration of macromolecular interaction. Certainly this function has yet to receive sufficient recognition in the field of thermodynamics. After applying it in studies of ribonuclease refolding and protein-protein interaction, we predict that this new state function will eventually supplant the GibbsHelmholtz expression in thermodynamic analysis.

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Uncovering the innate thermodynamic quantities in protein unfolding

Chun

1999

Int. J. Quant. Chem.

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Unwinding the Double Helix: Complete Equation for Chemical Equilibrium

Cited by 7 publications

References 8 publications

Isokinetic Relationship, Isoequilibrium Relationship, and Enthalpy−Entropy Compensation

Isokinetic Relationship, Isoequilibrium Relationship, and Enthalpy−Entropy Compensation

Approximation of the Planck-Benzinger thermal work function in protein refolding in ribonuclease systems

Uncovering the innate thermodynamic quantities in protein unfolding

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