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Determining the thermal set point in interacting biological systems
Author(s) -
Chun Paul W.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a637-e
Subject(s) - cutoff , thermodynamics , gibbs free energy , thermal , enthalpy , entropy (arrow of time) , freezing point , statistical physics , chemistry , physics , quantum mechanics
One of the more interesting discoveries in recent studies of biological thermodynamics concerns the way in which application of the Planck‐Benzinger methodology allows one to evaluate how the thermal set point of a biological system is established and maintained on a molecular level. Macromolecular interactions will always exhibit a negative minimum value of the Gibbs free energy change at a well‐defined temperature, , which may be defined as the thermal set point. Each interacting biological system will have its own unique value of where the bound unavailable energy TΔS° = 0. In the human body, that thermal set point is 37 degrees Celsius. At this point, ΔH°(T S )(−) = ΔG°(T S )(−) minimum , the maximum work can be accomplished and the system is at its most stable. Application of the Chun method has demonstrated that there is a lower cutoff point, , where entropy is favorable but enthalpy is unfavorable and an upper cutoff, , above which enthalpy is favorable but entropy unfavorable. Only between these two limits, where ΔG°(T) = 0, is the net chemical driving force favorable for such biological processes as protein folding, protein‐protein or protein‐nucleic acid interaction and protein‐self assembly. In examining interacting biological systems, the thermal set point will vary from one organism to another, but the fact that the value of TΔS° = 0 will not.