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The relative reactivities of these thiols with other disulfide substrates might differ depending on complementary/repulsive thiol disulfide binding interactions that could enhance or deplete reactivity accordingly.
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Molecular docking studies were carried out to investigate the mode of binding as well as important binding site interactions that could possibly explain the increased CA inhibition observed for chloro triazine derived compounds.
Many of these genes are involved in DNA binding or protein protein interactions that could regulate the lytic or lysogenic state of the phage (Kolkhof et al. 1992; Tourasse and Kolsto 2008).
This indicates a potential disruption of protein interactions that could influence binding or the stability of binding.
In support of this, heparin was observed to compact the microtubule binding domain and to break long-range interactions that could prevent sampling of aggregation-competent conformers.
Afterward, we selected a subset of 109 interactions that could be confirmed by the presence of a phylogenetically conserved binding site of the respective regulator.
Site-specific binding of dimeric [4Fe-4S] FNR to DNA represents another interaction that could affect potentially the cluster conversion reaction.
The significance of this tight clustering is unclear at present, as these aa's have not been associated with known interactions, but this could form a new unidentified binding site that could have a critical role in telomere protection.
Intuitively, the negative interaction data provide qualitative information on the contribution of amino acids to binding affinity that could improve quantitative prediction.
These authors also proposed that binding of intrinsically unstructured proteins benefits from a large interaction surface that could compensate for the entropic cost of binding.
Since the conformation of these individual domains could be altered under physiological conditions, we evaluated the possibility that these binding interactions could be different in muscle expressing full-length dysferlin.
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