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Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site.
DNA binding experiments indicate that both mutants retain the ability to bind AP site-containing DNA with similar affinity as wild-type Tdp1 (Fig. 5A).
LNA binding experiments indicate that unwinding of this helix induces a major structural rearrangement throughout the frameshift domain.
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Protein binding experiment indicated that 1 3 could bind to bovine serum albumin (BSA) with moderate bonding via the static quenching mechanism.
Radioligand-binding experiments indicated that mtCXCL12 had an affinity for CXCR4 that was identical to the wild-type sequence (Fig. 1 A ).
Our results indicate that the B2 element of the extended NLS also encompasses acidic residues C-terminal to the basic residues implicated in pocket binding, and peptide array experiments indicate that these residues are required for Impα binding.
Our computational analysis and experiments indicate that binding of VA to proteins is consistent with the hydrophobic effect and the Meyer-Overton rule.
However, our experiments indicate that 14-3-3 14-3-3 14-3-3ences the cytoplasmic localization of LRRK2, as disruption of 14-3-3 binding by mutatinfluences/Ser caused LRRK2 theacytoplasmicithin cytoplocalization.
The competitive displacement experiments indicate that the binding sites resemble two different types of receptors, specific for estrogens and androgens, respectively.
Our experiments indicate that promoter-proximal binding may be important for T-box TFs to recruit RNAPII and induce mesoderm-specific transcription.
Rescue experiments indicate that catalytic activity and binding to the vesicle coat protein clathrin are essential for OCRL1 function in these processes.
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