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To enhance the substrate concentration and overcome the substrate-tolerance obstacle [14,19], the reaction was explored in the aqueous/organic biphasic system.
The possibility of using a long path length spectroelectrochemical cell to determine the rate constant and diffusion coefficient for a catalytic reaction was explored.
Analysis of the electrode reaction was explored using cyclic voltammetry, and chronoamperometry with a platinum micro-disk electrode, and bulk potentiostatic electrolysis and UV vis spectroscopy.
The mechanism of the forward reaction was explored and elucidated using steady-state kinetics by coupled enzyme-spectrophotometric assays and ITC.
The scope of this reaction was explored; substrates with different ring sizes, benzamide substitution patterns, substitution on the bicyclic core, and heterocyclic substrates were well tolerated.
The effect of each mutation in the Y93L/L367I variant on the enantioselectivity of kinetic resolution in the model reaction was explored by applying variants with single point mutations (Y93L and L367I).
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Different temperatures (400°C and 500°C) and times (10, 20, and 60 s) of reaction were explored.
The significance of the kinetics of the interfacial dissociation reaction is explored.
Using model complexes, the characteristics of alternative (associative) mechanisms that have been proposed for the metallophosphatase catalysed reaction are explored.
Eight possible reaction pathways including eleven reaction channels on both the singlet and triplet potential energy profiles for the title reaction were explored.
The stationary pattern forming capacities of the reaction are explored through a systematic design method, which is applicable to other bistable and oscillatory reactions.
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CEO of Professional Science Editing for Scientists @ prosciediting.com