A thermodynamic molecular switch in biological systems: ribonuclease S' fragment complementation reactions.
It is well known that essentially all biological systems function over a very narrow temperature range. Most typical macromolecular interactions show DeltaH degrees (T) positive (unfavorable) and a positive DeltaS degrees (T) (favorable) at low temperature, because of a positive (DeltaCp degrees /T). Because DeltaG degrees (T) for biological systems shows a complicated behavior, wherein DeltaG degrees (T) changes from positive to negative, then reaches a negative value of maximum magnitude (favorable), and finally becomes positive as temperature increases, it is clear that a deeper-lying thermodynamic explanation is required. This communication demonstrates that the critical factor is a temperature-dependent DeltaCp degrees (T) (heat capacity change) of reaction that is positive at low temperature but switches to a negative value at a temperature well below the ambient range. Thus the thermodynamic molecular switch determines the behavior patterns of the Gibbs free energy change and hence a change in the equilibrium constant, K(eq), and/or spontaneity. The subsequent, mathematically predictable changes in DeltaH degrees (T), DeltaS degrees (T), DeltaW degrees (T), and DeltaG degrees (T) give rise to the classically observed behavior patterns in biological reactivity, as may be seen in ribonuclease S' fragment complementation reactions.
Chun
P W
PW
Department of Biochemistry, University of Florida College of Medicine, Gainesville, Florida 32610-0245 USA. pwchun@biochem.med.ufl.edu
D019943:Amino Acid Substitution; D009113:Muramidase / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D011489:Protein Denaturation; D012260:Ribonucleases / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics
D010446:Peptide Fragments; D012260:Ribonucleases; C022542:ribonuclease S; D009113:Muramidase