what is the difference between thermodynamic and kinetic stability?

Answer 1

Thermodynamic stability means that making a product involves an exothermic reaction. Kinetic stability means that there is a barrier to the reaction actually starting, called an activation energy barrier.

Answer 2

Thermodynamic Vs Kinetic Stability

Answer 3

Put simply, kinetic stability is stability that occurs because a particular state cannot be caused to change without the input of a significant amount of additional energy. This is callled a 'kinetic barrier'. Thermodynamic stability is more fundamental: A thermodynaically stable state cannot be altered to a less thermodynamically stable state, without a net input of energy. The human body, for example, based on thermodynamic stability alone, should spotaneously combust in the atmosphere. it does not, because there is a kkinetic energy barrier to that reaction.

Answer 4

Thermodynamics is a branch of physics studying processes involving transfer of thermal energy (heat). In mechanics, energy transfer results from a force which causes displacement, the product of the two being the amount of energy transferred. In a similar way, thermodynamic systems can be thought of as transferring energy as the result of a generalized force causing a generalized displacement, with the product of the two being the amount of energy transferred. These thermodynamic force-displacement pairs are known as conjugate variables. The most common conjugate thermodynamic variables are pressure-volume (mechanical parameters), temperature-entropy (thermal parameters), and chemical potential-particle number (material parameters).

Because thermodynamics is basically statistical mechanics of large ensemble of identical particles (atoms, molecules, electrons, photons, etc) then all laws of thermodynamics mathematically follow from laws of statistics of identical particles.

Kinetic stability as a mechanism for protease longevity
Erin L. Cunningham, Sheila S. Jaswal, Julie L. Sohl*, and David A. Agard
Graduate Group in Biophysics, Howard Hughes Medical Institute, and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0448


The folding of the extracellular serine protease, -lytic protease (LP; EC 3.4.21.12) reveals a novel mechanism for stability that appears to lead to a longer functional lifetime for the protease. For LP, stability is based not on thermodynamics, but on kinetics. Whereas this has required the coevolution of a pro region to facilitate folding, the result has been the optimization of native-state properties independent of their consequences on thermodynamic stability. Structural and mutational data lead to a model for catalysis of folding in which the pro region binds to a conserved -hairpin in the LP C-terminal domain, stabilizing the folding transition state and the native state. The pro region is then proteolytically degraded, leaving the active LP trapped in a metastable conformation. This metastability appears to be a consequence of pressure to evolve properties of the native state, including a large, highly cooperative barrier to unfolding, and extreme rigidity, that reduce susceptibility to proteolytic degradation. In a test of survival under highly proteolytic conditions, homologous mammalian proteases that have not evolved kinetic stability are much more rapidly degraded than LP. Kinetic stability as a means to longevity is likely to be a mechanism conserved among the majority of extracellular bacterial pro-proteases and may emerge as a general strategy for intracellular eukaryotic proteases subject to harsh conditions as well.