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The resistance of the coating against biogrowth was studied by quantifying the number of microorganisms on the coating surface after immersing to natural sea water containing microorganisms.
The molecular regulation of swimming-enhanced muscle growth was studied by quantifying the expression of fourteen muscle growth marker genes after long-term training.
Thymic function was studied by quantifying the production of TRECs in peripheral blood mononuclear cells (PBMC) by real-time quantitative PCR in a LightCycler system (Roche Molecular Biochemicals, Mannheim, Germany) [ 5].
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Ceramic damage is studied by quantifying the size and distribution of fragments in recovered sample.
The influence of VSL#3 to satiety hormones were studied by quantifying the two most well- known members, pancreatic polypeptide (PP) and polypeptide YY (PYY).
Secondly, allometric differences in crown construction patterns between environments were studied by quantifying 10 traits in 20 individuals from each environment.
Moreover, the primary heat source and hence controlling structure for heat transport of the geothermal reservoir is studied by quantifying the uncertainties in its temperature, depth, and shape and their influence on the heat transport processes.
The effects were studied by quantifying changes in transcripts with gene-sequence primer pairs for a suite of gene responses (AhRα, ARNT, CYP1A1, CYP3A, UGT and GST) belonging to the xenobiotic biotransformation system.
The functional groups contributing to nitrogen removal in the bioreactor were studied by quantifying nirS and nirK present in denitrifying bacteria, nosZI and nosZII genes from the nitrous oxide – reducing community, and a taxa-specific part of the16S rRNA gene for the anammox community.
Density-dependent selection can also be studied by quantifying effects of density on fitness in populations of individuals with different genetic origins.
The α-helix of peptides 11438, 33207, 33208 and 33210 were built hydrated and minimized at 310°K by using QUANTA program; then the α-helix stability was studied by molecular dynamics using CHARMM, quantifying the mean number of hydrogen bonds that remains in the α-helix at 0.0, 0.5, 1.0, 1.5 and 2.0 ns during the molecular dynamics of the peptide in water at 310°K.
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