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Furthermore, the previously proposed binding of a third zinc ion close to the active site of IMP-6 mutant S121G was corroborated by our simulations.
These data clearly show that higher NaCl concentrations prevent binding of a third DBD molecule but still allow for formation of at least a 2 1 complex even when a Rap1 recognition sequence is present in the substrate.
In our study, we investigated the binding of a third ssDNA oligonucleotide fragment (i.e., 5′-CTGTTG-3′) to N- HvGR-RBP1, in which the CTG element was retained but the other nucleotides scrambled.
Incorporation of two deoxynucleotides, followed by translocation onto the next templating base (position 0 in Figure 2C) and binding of a third dGTP molecule is required in order to trigger formation of the crystal lattice, capturing Pol α in an actively copying conformation.
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Therefore, the binding of AZ1 to ODC occludes the binding of a second molecule of ODC to form the active homodimer.
The structure shows cAZ1 binding to ODC, which occludes the binding of a second molecule of ODC to form the active homodimer.
Our crystal structure undoubtedly shows the association of AZ1 with one monomer of ODC, which occludes the binding of a second ODC monomer to form the catalytically active ODC homodimer.
The functional monovalency of these two independent anti-rodent TNF mAbs is presumably a result of steric hindrance from one TNF molecule binding to one Fab arm that prevents binding of a second TNF molecule to the other Fab arm.
The result is that the binding of a second substrate molecule to the second subunit of the enzyme differs in strength or velocity from that of the first, the third from the second, and so on.
The electrogenic interaction of the first Na+ ion with NaPi-IIa/b at a postulated Na1 site is accompanied by charge displacement, and Na1 occupancy subsequently facilitates binding of a second Na+ ion at Na2.
These regions may potentially be involved in binding of a second adaptor, for example TRIF.
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