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The bioactive layer incorporating epidermal growth factor (EGF) molecules was subsequently electrospun on the antibacterial layer.
The pattern of molecules was subsequently assembled to align with the Illumina-based assembly to achieve sequence extension.
The optimal number of overlapping lipid molecules was subsequently calculated and removed followed by lipid expansion (inflation) and alternating twenty steps of deflation and energy minimization to allow the peptide to be embedded within the bilayer using inflateGRO2.
An Fe2+-binding site located on the inner surface of the subunit, ∼10 Å away from the ferroxidase site and coordinated by His46, Asp50, and three water molecules, was subsequently identified.[ 3c] Disruption of this site severely inhibited mineralization, consistent with an important role in electron transfer from Fe2+ ions in the cavity to the ferroxidase site.
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These molecules were subsequently electro-polymerized accompanied with simultaneous electro-reduction of exfoliated GO.
These molecules are subsequently reduced with NADPH and the enzyme glyceraldehyde-3-phosphate dehydrogenase to give six molecules of Gal3P.
These molecules are subsequently further degraded to low molecular weight (LMW) oligonucleosome-sized fragments.
The DNA molecules were subsequently used as templates for in vitro transcription by T7 RNA polymerase.
The remaining single stranded cDNA molecules were subsequently amplified, and library construction proceeded as for non-normalized libraries.
POPS and PIP2 molecules were subsequently incorporated into the equilibrated POPC bilayer by exchanging them for POPC molecules; this procedure was implemented using an in house lipid exchange script [30].
These biotinylated C3b molecules were subsequently loaded onto small magnetic streptavidin beads that have a diameter of 2.8 μm (bacteria-sized) and a theoretical binding capacity of around 50,000 C3b molecules per particle (Fig. 1a).
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