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Introduction of the (RS -2-fluoropropionic acid at the N-teRS -2-fluoropropionic RS -2-fluoropropionicffinity by acidctor of atprox. 10.
Thus, the specific binding affinity and nonspecific binding affinity by a protein typically converge at very low salt concentrations and diverge at high salt concentrations as we observe for the MBD (Table 1).
Deletion of this Myb domain reduces telomeric dsDNA binding affinity by a factor of 2.9 (Table 1), eliminates telomeric binding specificity, and grossly alters DNA binding properties compared to those of full length TRF2.
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Specifically, mutations in surface charges away from the binding interface can elicit new on-pathway encounter complexes, increasing their binding affinity by an order of magnitude.
Exquisite dependence on eIF4G concentration for translation initiation may result from reduced eIF4G binding affinity by an mRNA, or from more complex indirect effects on translation factors and ribosome affinity.
This is consistent with competitive inhibition in which the inhibitor interferes with the catalytic properties of enzyme by affecting substrate binding affinity by conferring a Ki of 2.7 mM.
It may increase VP1-receptor binding affinity by forming an ionic bond.
To improve the accuracy of binding site search, traditional methods impose filters such as phylogenetic footprinting information and transcription factor-DNA binding affinity by setting the p-value in a ChIP-chip experiment.
Substitution of Glu pTyr+2) with Asn in pYEEI and pYEEV (to yield pYENI and pYENV, respectively), or of Ile pTyr+3) with Val in pYEEI and pYENI causes a decrease in binding affinity by approximately 1.8 kJ/mol.
This screening leads to a decrease in the dendrimer binding affinity by orders of magnitude.
Interestingly, these investigators find that TM251 binds to HDAC8 at two sites in a cooperative manner; additionally, TM251 modestly enhances inhibitor binding affinity by approximately 2-fold.
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