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By following this rational design concept of targeting multiple structural water molecules as binding partners for small organic molecules, we could enhance the binding affinity of our rationally designed phthalimide scaffold by a factor of 20.
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Removing BMH2, in contrast, removes a smaller proportion of binding partners for Rad53, thus resulting in a milder suppression effect on cdc13-1.
Based on these initial findings, we screened a fluorescent small molecules based library in order to identify fluorescent binding partners for the DAPK catalytic domain, which could serve as reporters of the protein dimerization state.
We used yeast two-hybrid analysis to identify potential protein binding partners for human TTP (hTTP).
Here, our focus was on using structural water molecules as binding partners for novel small‐molecule modulators.
These two proteins may represent novel binding partners for Tspan9.
Electrostatic interactions can facilitate macromolecular recognition by enhancing the collision frequency of the binding partners and by orienting the binding partners for subsequent short-range interactions.
At least 20 proteins (besides G-alpha subunits) have now been identified as direct binding partners for RGS proteins, and additional binding partners remain to be found [ 4].
Their differences define the concentrations of binding partners for effectors whose binding site phosphorylations are described in different layers.
Unfortunately, in the literature there are no identified binding partners for the SH3 domain of Caskin1.
The main nuclear binding partners for Yap and Taz are the Tea domain (Tead) transcription factors.
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