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Upon pre-treatment with IBR1/2, immobilized RAD51 lost the ability to bind BRC repeat (Fig 1D and E), whereas neither compound affected the binding of RAD51 to immobilized BRC repeat (Fig 1F and G).
They observed that the size of SiNP drastically affected the binding of 37%% of the identified proteins.
Base substitutions up to one helical turn from the center of the AP-1 site affected the binding orientation.
The aryl groups at N9 position affected the binding affinities between compounds and TAR RNA, showing some specificities of aryl groups to TAR RNA.
Neither glutathione nor the pro-oxidant tert-butylhydroperoxide affected the binding of [3H]-triptolide to the nuclear protein, ruling out a general oxidant effect.
Surprisingly, wild-type CS/DS significantly reduced the binding of Fgf7 to keratinocytes in a concentration dependent manner unlike the Dcn−/− CS/DS that only affected the binding at higher concentrations.
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The increasing temperature could affect the binding of small molecules and protein for different quenching types.
On the other hand, two single mutations (S346A and T347A) did not affect the binding outcomes.
(E) PBZ treatment does not affect the binding of HCV to host cells.
However, the terminal substituents were found to hardly affect the binding selectivity in the studied cases.
Finally, species differences are also a vital factor that can affect the binding of active components binding and plasma proteins.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com