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Fluorescence complementation and catalytic activity occurred when both halves of the fluorescent protein were fused to the respective amino-terminus of both sGC subunits.
Bimolecular fluorescence complementation.
The Bimolecular fluorescence complementation (BiFC) assay indicated the interaction between OsRLCK107 with OsCERK1 (Fig. 3a).
This assay enables quantitative analysis of PDZ domain-mediated protein clustering using bimolecular fluorescence complementation (BiFC).
A novel GFP-based bimolecular fluorescence complementation (BiFC) system also identified Y1 receptor-β-arrestin complexes.
To monitor the light-controlled formation of the assemblies in vivo, a fluorescence complementation assay was also performed.
The assembly of the fusion proteins in E. coli was monitored using the fluorescence complementation assay (Gao et al. 2015).
Yeast two-hybrid and bimolecular fluorescence complementation experiments provide support for physical interactions among the OsWRKYIIa proteins (Y. Seo et al., in preparation).
We confirmed the in vivo interaction using Bimolecular Fluorescence Complementation (BiFC) methods that detect interactions between two proteins in living cells.
To validate the protein protein interaction between LhSorTGA2 and LhSorNPR1, the bimolecular fluorescence complementation (BiFC) assay was performed using vectors described previously.
Dynamic light scattering (DLS), fluorescence complementation, scanning electron microscopy (SEM), optical density measurements (OD600), and enzyme activity assays were performed to study the mechanisms involved.
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