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The science of thermodynamics tells us that closed systems tend toward equilibrium, toward dullness, toward entropy.
Alcohol compounds bearing electron-donating groups allow to displace the equilibrium toward ester formation.
The aggregation of denatured protein gradually shifts the protein equilibrium toward increasing amounts of denatured and ultimately aggregated protein.
The electrochemical removal of the unwanted ions from the exchange medium drives equilibrium toward greater exchange of the desired ion.
The concentration of hydrogen increases in the liquid phase with increase in hydrogen pressure and would drive the reaction equilibrium toward 1,2-PDO formation.
Since the reaction involved in biodiesel is reversible, one would expect that increasing the amount of methanol would shift the reaction equilibrium toward the products [45].
In addition, tuning the acid/base properties leads to a shift of the equilibrium toward a non-charged (acid) form that further reduces the viscosity.
The selective permeation of methanol through each polymer membrane shifted the chemical equilibrium toward the favorable direction in the MTBE decomposition reaction.
Secondly, for model proteins with two competing native states, cotranslational folding tilts the apparent equilibrium toward the state with a more local-contact dominant topology.
The hydrogenation of the dehydration products shifts the dehydration hydration equilibrium toward the dehydration pathway and leads to highly selective CO cleavage.
High temperature and the presence of tin catalysts are also favorable factors, while, as expected, dilution shifts the equilibrium toward the formation of high yields of cyclic oligoesters.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com