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It inhibits bacterial protein synthesis by binding of each component to a different site on the 50S subunit of the bacterial ribosome, dalfopristin leading to a conformational change in the ribosome which increases the affinity of the ribosome for quinupristin.
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In this context, the relative abundance and binding affinity of each component could be regulated independently [cf. 57], [58], ultimately leading to either changes in PSD composition or its complete disassembly.
The type 5 isoform is a homodimeric enzyme with a single catalytic binding site and regulatory binding site in each component of the dimer (Blount et al. 2004).The catalytic site hydrolyzes cyclic GMP to inactive 5′-guanosine monophosphate.
Membrane orientation of the reconstructed bR-PLs or FoF1-PLs was assessed by observing the binding affinity of each protein component to Ni-NTA Magnetic Beads, and 41.3 mM of lipid mixture (SoyPC extract/cholesterol with the molar ratio of 70 30) was reconstituted with either FoF1 or bR at the protein concentration of 0.2 µM.
The classical complement system is activated following the binding of complement component C1 to the immune complex.
Hydralazine, but not its acetylated metabolite MTP, blocked covalent binding of complement component C4.
These represent the binding of a component L to a microstate.
SEMBL inhibited DNA binding of NF-κB component p65 in vitro.
A fluorescence polarization assay has been described for binding of component 2 to its cognate DNA sequence [ 53].
Activation of the classical complement pathway requires binding of the complement component C1q to the mAb Fc.
The simultaneous binding of both components explains the specificity of the receptor for haptoglobin-haemoglobin complexes over each individual component.
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