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Here, we used PapI and an isolated DNA-binding domain construct of Lrp to show that there is a DNA co-recognition mechanism by which both proteins acquire enhanced affinity to the distal pap site DNA, to which neither of them binds to an appreciable extent without the other.
This unique interfacial microstructure might contribute to the strong retention of volatile compounds due to steric barrier and enhanced affinity to those lipophilic volatiles.
In contrast, sulfur substitution of the phosphoryl oxygens, either one (monothio) or two (dithio) of the non-bridging oxygen atoms, exhibit enhanced affinity to protein as well as resistance against nucleases in both cellular and plasma environments [39].
58 CAVATAK™ consists of the genetically unmodified coxsackie virus A21 which has an enhanced affinity to melanoma cells compared to normal cells.
This conception was based on the early finding that insulin glargine had an enhanced affinity to IGF-1 receptors when tested in a human osteosarcoma cell line (Saos/B10) with a preponderance of IGF-1 receptors and associated with increased mitogenicity (proliferation in an existing tumor cell line) (4).
Taking into account the peculiarities of the active-site flap cysteine in the urease catalysis and sulfhydryl group in urease activity, it could be inferred that ASB made contacts with the side chains of cysteine residues, especially sulfhydryl group, which was reflected in their enhanced affinity to the Cys-592.
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In all family members, the enediyne core is strategically decorated with a bioorthogonal "triggering" system and specific appendages that enhance affinity to the metabolite's target (DNA/RNA).
Multimeric compounds could have enhanced affinity due to statistical rebinding or simultaneous binding to receptors.
On the other hand, multimeric compounds could have enhanced affinity due to statistical rebinding: the receptor binding of one RGD unit will significantly enhance the local concentration of the second RGD unit in the vicinity of the receptor.
Aside from alanine mutations of AB loop residues that decrease affinity by modifying dissociation rates (e.g. Y1542), a novel mutation (E1544A) of the AB loop enhanced affinity by threefold compared to wild-type.
A recent study has enhanced affinity of an antibody fragment to the I-domain of the integrin VLA1 [ 45] by about an order of magnitude by mutating four residues at the antibody part of the interface.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com