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Therefore, the occupation of the anions in YanI probably hampers the binding of Na+/K+ to SMC element.
It was shown by Broothaerts et al. [ 2] that in the test sequence of the Adh1 reference gene, a single nucleotide polymorphism hampers the binding of the reverse primer.
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However, PEGylation did not hamper the binding of the αN Ab to the caleosin.
For instance, HDL might hamper the binding of LPS to its receptor at the cell surface, as reviewed by Wu et al. [ 39].
Consequently, the addition of organic additives seems to hamper the binding of the more bulky substrate benzaldehyde to the donor binding site more than the acceptor binding site, yielding smaller 2-hydroxy ketones.
Thus, our data are compatible with the hypothesis that this QTL alters the molecular interaction mechanism described by Hemmes et al. (2009) in hampering the binding process, for instance, in blocking the loading of siRNAs into RNA silencing effector complexes.
Our data strongly suggest that: i) Cys PEGylation does not hamper the binding of the αN Ab to the caleosin but impedes the binding of the FL Ab, and ii) the FL Ab only recognizes the C-terminal part of the protein.
Our results may indicate a threshold effect, since there is no discernible decrease in birth weight below a maternal PCB concentration of less than 25 μg / L. Assuming an endocrine mode of interference of PCB, a threshold effect is plausible since PCB may hamper the binding of hormones to their receptors [ 52].
Similarly, both Z. sapae HOs conserved a few amino acid residues (i.e., D222, G223, R286, K308, D333, K417), that, once replaced in S. cerevisiae HO, hampered the binding and/or endonuclease activities in vivo or in vitro, or are considered functionally relevant by homology modeling with PI-SceI (Meiron et al. 1995; Ekino et al. 1999; Bakhrat et al. 2004; Ezov et al. 2010).
Considering both the structural data and results of site-directed mutagenesis obtained here, together with the previous mutagenesis study of Ca2+-coordinating residues Asp94 and Glu99, which severely hampered the ice binding [23], we propose that the ice-binding site of hAFP consists of Asp94, Thr96, Thr98, and Glu99 that form a relatively flat surface to interact with ice (Figure 8AB).
The steric hindrance of the coalescent headgroups hampers the penetration of the complexed moieties into the binding pockets of ChTB, lowering its binding probability to GM1.
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