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The cellular levels of all proteins were significantly correlated to each other (P < 0.001 for each correlation).
Uncertainty bounds were calculated for each correlation.
Note that autoaips must be run separately for each correlation pass and each requires its own directory.
For OSFs, further comparisons with the previous empirical correlations from literatures are conducted to verify the accuracy of each correlation.
Each correlation is characterized by uncertainties, i.e. it returns an approximate value of the variable that it aims at predicting.
However, for reasons discussed fully in Appendix 13.7, wtransform does not compute significances directly, but rather compares each correlation value with a threshold correlation value.
For both empirical correlations, p-values less than 0.05 were easily obtained, inferring the statistical significance of each correlation.
Two versions were developed for each correlation: one that assumes a priori knowledge of the local heat flux and another that does not.
Firstly, the original values of parameters of each correlation were used to reproduce the experimental data, finding that most of them failed to do so.
Damkohler number analysis is used to determine degree of equilibrium for each correlation and extent of error introduced by assuming local equilibrium between the NAPL and aqueous phases.
Each correlation was derived for certain conditions.
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CEO of Professional Science Editing for Scientists @ prosciediting.com