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This change in the flexible structures of AM-2 and AM-3 could have resulted in decreased binding of these peptides to zwitterionic lipid bilayers and increased damage to mixed lipid bilayers containing acidic phospholipids.
To more accurately reflect the situation in normal brain, the binding of these peptides to adult neurons was also determined in a mouse brain slice model.
The first is that MDM2 modulates the binding of these peptides as has been shown elsewhere [ 20, 38].
Taking into account that peptide 11438 sequence belongs to the gH binding region we were interested in determining the binding of these peptides to different type of cells.
The natural MSH peptides have a conserved sequence, His-Phe-Arg-Trp, which plays an important role in the binding of these peptides to specific melanocortin receptors.
The binding of these peptides was observed to cause oligomerisation of luminal domains, with the implication that this leads to UPR activation.
Similar(51)
This hypothesis was then examined by studying the bindings of these peptides with their receptors in mammals and conflicting results were reported.
The binding properties of these peptides were first examined using an opioid binding assay.
Since PlyG peptides demonstrated specific binding to both B. cereus-4342 and B. anthracis-Sterne in the dot blot assay, we further evaluated the binding ability of these peptides to the bacteria in an ELISA based assay.
However the binding affinities of these peptides did not exceed substantially that of NCPERIITL, the most affine peptide tested in the original peptide set (pBL50(exp) = 7.120).
Further, the experimentally-determined binding affinities of these peptides were also not substantially lower than that of the index peptide (Table 3b).
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