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Using X-ray photoelectron spectroscopy (XPS), the properties of individual domains of the chimeric peptides were evaluated for their binding activity toward the Ti surface.
Using phage display technology three variants were selected from a random library of the bilin-binding protein (BBP), a prototypic lipocalin, which exhibit binding activity toward the nonsymmetric phthalic acid ester.
The highly basic C termini of the mutant CALR proteins obviously have reduced binding activity toward the Ca2+ cation.
Likewise, N-RPGR with the truncation, Q236X, exhibits still some binding activity toward the RID of RPGRIP1α1 and such activity extends beyond the conserved RHD as supported by the partial loss of binding activity caused by class IV mutations, such as G43R and G43E.
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In each iteration, a comparatively small batch of compounds is screened for binding activity toward this target.
Notably, the shorter the sequence of ORF15, the lower is the binding activity toward RID of RPGRIP1α1.
The secreted product exhibited the specific binding activity toward soluble human Fas receptor extracellular domain human IgG1-Fc domain fusion protein, and the receptor ligand complex was immunoprecipitated by Protein A conjugated agarose-gel beads.
Herein, we present a refined version of the Herbochip® platform and report successful identification of the binding activity toward TNF-α in 46 out of 82 selected herbal extracts.
All components in peaks II and III were found in the precipitated samples obtained in the receptor-mediated co-immunoprecipitaion experiments using either wild-type or the mutant hFasRECD-T-Fc, which suggested that the cross-linked products in peaks II and III retained the binding activity toward hFasRECD.
The details of site-specific chemical modifications of this mutant with maleimide group containing compounds as well as the characterizations of the purified reaction products concerning binding activity toward hFasRECD and cytotoxic activity against a cancer cell line will be presented.
Either tag-free hFasLECD containing untrimmed or trimmed N-glycan exhibited virtually identical binding activity toward mutant hFasRECD-T-Fc lacking N-glycosylation site within the hFasRECD part with the activity toward wild type hFasRECD-T-Fc, suggesting N-glycosylation in both hFasLECD and hFasRECD is not a prerequisite for protein – protein interactions between hFasLECD and hFasRECD.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com