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NMR experiments confirmed binding to the A-site for some compounds.
The existence of the S-state neamine may facilitate binding of neamine-like aminoglycosides by favorable entropy of binding to the A-site of 16S ribosomal RNA, suggesting that novel aminoglycoside compounds carrying a S-state neamine pharmacophore can be developed.
Tetracycline inhibits binding of RNA to ribosomes mainly by influencing binding to the A-site although some reports implicate binding of Ac-Phe-tRNA to the P-site 57, 58.
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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.
The high activity of amikacin observed in this study may be attributed to the presence of the aminohydroxybutyryl group, which generally prevents the enzymatic modification of amikacin at multiple positions without interfering with binding to the A site of rRNA [25].
Therefore since binding to the A site by the tRNA-EF-Tu complex is reversible, there will be an inherent bias for misincorporation by misacylated tRNA Pro relative to other misacylated tRNAs.
Tobramycin affects protein synthesis by binding to the A site of the 30 S ribosomal subunit [ 4], interacting with the A1408 residue (E. coli numbering) of the decoding site 16 S rRNA [ 5].
Its primary antimicrobial effect takes place by direct steric hindrance by binding to the A site in the 30S subunit, thus hindering the movement of transfer RNA and inhibits peptide elongation [ 42].
Peptidyltransfer assays using Ac-[14C]Phe-tRNA and puromycin, and equilibrium binding studies of [14C]Phe-tRNA binding to the ribosomal A-site, and of Ac-[14C]Phe-tRNA to the ribosomal P-site were carried out as previously described [47].
In yeast, EF-3 interacts with both ribosomal subunits and facilitates elongation factor EF-1-mediated cognate aminoacyl-tRNA binding to the ribosomal A-site [ 39].
However, the correlation of inhibition activity with binding strength to the A-site was limited.
More suggestions(15)
binding to the integrin
binding to the probe
binding to the peptide
binding to the consensus
binding to the site
binding to the metal
binding to the genome
binding to the transmembrane
binding to the matrix
binding to the zinc
binding to the end
binding to the fibrinogen
binding to the channel
binding to the resin
binding to the host
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