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Exact(4)
Of particular note is the result that the couple M y resulting from binding is the same for both elastic and self-ligation.
However, the model relies on the assumptions that: (1) a reference region devoid of specific binding exists, and (2) the nonspecific binding is the same in both the reference and target regions.
In the case that kon for rGTP binding is the same as kon for dGTP binding and the increase in Kd value for rGTP relative to dGTP is solely attributable to the increase in koff, we calculate koff = kon Kd (for rGTP) = 11607 s–1, which can be viewed as an upper bound for the rGTP dissociation rate for the D12A/D66A mutant.
In the case that kon for rGTP binding is the same as kon for dGTP binding and that the increase in Kd value for rGTP relative to dGTP is entirely attributable to the increase in koff, the dissociation rate for rGTP would be koff = kon Kd (for rGTP) = 36346 s–1, which can be viewed as an upper bound for the rate of dissociation of rGTP from wild-type Φ29 DNAP complexes.
Similar(56)
Our results show that the protein regions responsible for the nucleic-acid binding are the same as those previously described to be implicated in NAC activity.
Analysis of the sequence derived from the whiB6 promoter (WB6) by ITC showed the requirements of two motifs for PhoP binding were the same as those of RD6.
Lea and French [ 81] found that while the K D for DHT AR binding was the same in carcinomas as in normal tissue, the actual on/off rates were much slower.
The relative protein content was estimated assuming that antibody binding was the same for phospho- and dephospho-MRLC and corrections made for offset and saturation errors as described [ 10].
Nevertheless, the conclusion reached there of two binding sites is the same as reached here with a more extensive range of much tighter binding species.
The swinholide A actin binding site is the same as that targeted by toxins of the trisoxazole family and numerous actin binding proteins, highlighting the importance of this site in actin polymerization.
It is assumed that binding to individual phospholipids is non-co-operative and that the adsorption energy at each binding site is the same for the protein (adsorbate).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com