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Linear correlations between the predicted binding scores and the experimentally measured binding affinities were observed.
Of the ligands tested, the highest binding affinities were observed for BMP2 with preferred binding to the type I receptors BMPR-IA (apparent KD: 0.8 nM) and BMPR-IB (2.7 nM) and for the GDF5 BMPR-IB interaction (1.3 nM), whereas activin A showed preferential bindinGDF5 BMPR-IBe interaction ActR-IIB with similarly high binding affinities (2.1.3M) (see Table 1).
Similar(58)
Control studies on AMP binding relative to ATP are also shown in the Supporting Information, wherein similar binding affinities are observed to be consistent with literature results.
The highest binding affinities are observed with full exposure of the aptamer sequence in the loop, while duplex formation reduces binding affinity most likely due to the thermodynamics of DNA base pairing.
No differences in receptor binding affinity were observed, and all samples demonstrated similar in vitro bioactivity.
All three mutants bound to PG like the wild-type, and no significant differences in the binding affinity were observed.
Importantly, such experiments revealed the complex nature of TF-DNA interactions, whereby the effects of nucleotide changes on the binding affinity were observed to be context dependent.
No differences in binding affinity were observed for partial blocking of the 5′ vs 3′ aptamer sequence ends in this study.
A significantly high binding affinity was observed for the PKR-inhibitor to the MARK4 variants.
The result showed that biotin-As bound to PML-RARA, similar binding affinity was observed with PML-RARA-L217F and S220G (Fig. 1D and 1E).
A considerable enhance in the binding affinity was observed, when compared with the zwitterionic PC, with a Kd of 0.04 µM.
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