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The binding analysis using a Job plot suggested that sensor 1 formed a 1 1 complex with Fe3+.
The binding analysis using a Job plot suggested that PB-CX[4] formed a 1 2 complex with Hg2+.
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cDNAs encoding Bam32 and TAPP1 were cloned into pGEX-4T-2 (Amersham) to obtain the production of Bam32 and TAPP1 GST-fusion proteins for the phospholipid-binding analysis using a protein-lipid overlay.
The binding properties of the mutant HAs were quantitatively characterized using a dose-dependent direct glycan-binding analysis using a glycan array platform.
To test, whether APP and LRP4 interact directly, analogous to the interactions of APP with LRP1 (Kounnas et al., 1995) and Apoer2 (Hoe et al., 2005), we performed a binding analysis using recombinant APP and LRP4 fusion proteins.
According to a saturation binding analysis using PAZ6 adipocytes, the β3-AR appears to be the most abundant β-AR subtype.
Real-time binding analysis using surface plasmon resonance (SPR) was conducted on a Biacore S200 instrument (GE Healthcare, USA) at 25°C.
DNA binding analysis using yeast one-hybrid assay revealed that GmGT-2A could bind to GT-1bx, GT-2bx, mGT-2bx-2 anD1D1 whereas GmGT-2B could bind to the latter three elements.
The binding analysis using Job's plot suggested 1 1 stoichiometry for the complexes formed for Hg2 +.
The binding analysis using Biacore showed the association and dissociation parameters of K46E mutant that were optimized with IgM.
The binding analysis using fluorescence spectroscopy suggested that the complexation between BLG and four nutraceutical models including β-carotene, folic acid, curcumin and ergocalciferol occurred under all conditions but varied as a function of pH and nutraceutical type.
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