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In chemistry, chemical stability is the thermodynamic stability of a chemical system, in particular a chemical compound or a polymer. [1] Colloquially, it may instead refer to kinetic persistence , the shelf-life of a metastable substance or system; that is, the timescale over which it begins to degrade.
Non-equilibrium thermodynamics is a branch of physics that studies the dynamics of statistical ensembles of molecules via unstable states. Being "stuck" in a thermodynamic trough without being at the lowest energy state is known as having kinetic stability or being kinetically persistent.
The term is used to describe a transient chemical species.As a general example, if a molecule exists in a particular conformation for a short lifetime, before adopting a lower energy conformation (structural arrangement), the former molecular structure is said to have 'high lability' (such as C 25, a 25-carbon fullerene spheroid).
The kinetic isotope effect is the difference in the rate of a chemical reaction when an atom in one of the reactants is replaced by one of its isotopes. Chemical kinetics provides information on residence time and heat transfer in a chemical reactor in chemical engineering and the molar mass distribution in polymer chemistry.
This equation explained the new, non-classical fact that an electron confined to be close to a nucleus would necessarily have a large kinetic energy so that the minimum total energy (kinetic plus potential) actually occurs at some positive separation rather than at zero separation; in other words, zero-point energy is essential for atomic ...
The kinetic process of destabilisation can be rather long (up to several months or even years for some products) and it is often required for the formulator to use further accelerating methods in order to reach reasonable development time for new product design.
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Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.