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Therefore Gly to Val change could induce conformational changes in the peptide chain and these changes might hinder the binding of PFN1 to actin.
With this methodology it is possible to identify fully complementary mAb pairs that would not sterically hinder the binding of each other to the same protein, e.g. for establishing a highly sensitive sandwich ELISA for PrPC and/or PrPSc.
One possible explanation is that full-length MUC1 contains a self-aggregation domain that likely contributes to the protein's characteristic clustering and could sterically hinder the binding of ligands to the adjacent region which is the Anti-MUC1* epitope.
The combined four mutations F151S, A152S, F714S, F717S are therefore sufficient to hinder the binding of CaM to hEAG1 (p>0.05) BD-C1 and other auxiliary sites can still be involved in the binding mechanism in a cooperative manner.
Our studies show that the disruption of BD-N and BD-C2 is sufficient to hinder the binding of CaM to full-length hEAG1, although we can also not exclude the possibility that BD-C1 is involved in CaM binding in a cooperative manner.
The C-terminal sequence SCRCMS to RQVHSIIRRHHHHHH lies in proximity to the loop 2 in the site 1 receptor binding interface of VEGF-C (Figure 6) and binding of anti-VEGF-C to this region could therefore also sterically hinder the binding of VEGF-C to its receptors.
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We observed an unexpected effect of a conserved mouse human framework position (L37) that hinders the binding of the humanized scFv to antigen.
In M. musculus AChE, the Y337A (F330A) mutation decreased Ki almost 2700-fold, makitg it comparable to BChE [13], presumably because the side chain of Tyr337 sterically hinders the binding of ethopropazine via an interaction between the aromatic side chain of the residue and the diethylamino-2-isopropyl moiety of the inhibitor.
These binding sites can be inactive due to the occupancy of nucleosomes hindering the binding of the TF to the binding site in any genome.
This is likely due to the low concentration of IgA in the serum [ 26] and possibly through the binding of the more abundant IgG to antigen, sterically hindering the binding of IgA in the assay.
More interestingly, the nonsubstituted compound 12 shows even greater inhibition (IC50=27 n m), indicating that the methyl group hinders the binding of the pyridyl nitrogen in the active site.
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