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Full-length angiocidin bound polyubiquitin while three angiocidin recombinant proteins whose putative polyubiquitin binding sites were mutated either failed to bind polyubiquitin or had significantly diminished binding activity.
These mutant proteins were either unable to bind polyubiquitin or displayed greatly diminished binding activity while angiocidin bound with high affinity.
The double SIM mutant showed diminished binding and the N-terminal-Wss1 fragment didn't bind SUMO-PA at all, indicating that SIM-SUMO interaction still contributed to the binding.
IgGs lacking glycosylation at N297 have slightly lower stability as well as diminished binding to FcγRs, but with no apparent change in binding to FcRn or half-life.
Results: With the pooled sera, substitution of a single AA led to complete abrogation of IgE binding to 2 of 8 peptides and diminished binding in the remainder.
Overall, the products of reactions catalyzed by aminoglycoside resistance enzymes exhibit diminished binding to the A site of bacterial 16S rRNA, which correlates well with a loss of antibacterial ability in resistant organisms that harbor these enzymes.
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As previously mentioned, the basis for antibody cross-reactivity with EBNA-1 and dsDNA does not appear to be charge interactions since removal of the negatively charged amino acids from the carboxyl region of EBNA-1 does not diminish binding to this region (Figure 7).
Acidic residues (D) may be present, although they diminish binding affinity, while non-charged residues (N) have neither positive nor negative impact upon binding (16).
Thus, the Y254V mutation diminishes binding discrimination against rNTP relative to dNTP in two distinct ways: it increases the binding affinity for complementary rNTP while simultaneously decreasing the binding affinity for complementary dNTP.
25 To test whether the hydrophobic pocket is involved in peptide binding the assay was performed for both wild-type PBD and a double mutant (Y417A/Y421A), designed to diminish binding to the hydrophobic pocket.
The high degree of conservation in the cytoplasmic tail, with many Ser, Thr, and Tyr residues, is compatible with the important role that phosphorylation of these residues plays in regulating adhesive activity [ 73] and with the observation that cytoplasmic domain truncation of CD18 markedly diminishes binding of LFA-1 to ICAM-1 [ 52].
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