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The orientations of both IgG layers immobilized on the base recombinant protein Gs were analyzed by fluorescence microscope, atomic force microscope (AFM), and surface plasmon resonance (SPR).
Mathematical and physical concepts of ss (including sp) and Gs were analyzed, and empirical equations linking sp and Gs with various petrophysical parameters were obtained.
Clinical and epidemiological data and physical parameters of the patients were recorded and surgically removed GS were analyzed chemically and physically to identify the type of GS.
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After cooling the solutions were transferred to test-tubes and brought to volume using dilute HCl while sample splits of 0.25 g were analyzed.
The chemical environments of Ni-NiO/PDDA-G were analyzed by electron spectroscopy for chemical analysis/X-ray photoelectron spectroscopy (ESCA/XPS) using a Thermo VG ESCAlab 250 (Thermo Fisher Scientific, Waltham, MA, USA) equipped with a dual-anode (MgKα/AlKα) X-ray source.
Twenty samples (from 4.2 g to 13.8 g, with an average wet weight of 8.9 g) were analyzed.
Fatty acids composition of milk (10 mL), diets (1 g), and diced muscle (2 g) were analyzed by gas chromatography.
Data in A, B, E and G were analyzed by ANOVA with Bonferroni post-tests, *p<0.05, ***p<0.001, ns = not significant.
To determine whether inadvertent hydrolysis of BPA metabolites occurred, samples spiked with only BPA-G were analyzed for the presence of uBPA.
Probe sets enriched by 1.5-fold or greater in Pde1C-driven EGFP-positive cells compared with whole cortex (Supplemental Fig. 3 g ) were analyzed further.
The extracellular concentrations of PAA and penicillin-G were analyzed by an isocratic HPLC method using a Zorbax® column at 30°C.
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