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A fluorenylmethoxycarbonyl sulfonic acid (FMS) derivative of the 6-aminoquinazoline analog of AG1478, which was designed to have improved serum-binding properties, was shown by fluorescence analysis to bind with approximately 100-fold greater affinity than the parent compound.
Intermediate doses of 2.0 2.5 J/cm2 were shown to maintain particle structure and chemical reactivity, and cellular binding properties were similar to CPMV-WT.
Furthermore, the in vitro reconstitution of different barley Lhcb1 isoforms showed that, at least in the monomeric form, their spectroscopic and pigment binding properties were essentially identical [61].
The binding properties were analyzed in competitive binding, internalization, and cell surface retention experiments.
The hypothesized binding properties were tested experimentally.
Indeed, adaptative mechanisms including modified DAT binding properties have been shown following partial nigrostriatal lesions [32].
The calmodulin-binding and iPLA2 activating properties of the peptides were shown by Surface Plasmon Resonance and iPLA2 activity assays.
The calmodulin-binding and iPLA2-activating properties of the peptides were shown by surface plasmon resonance and iPLA2 activity assays.
Such membrane binding properties have recently been shown for arginine residues in the TAT signal [42].
It must be emphasized that rapid displacements of subsecond frequency might strongly influence receptor binding properties: indeed it was shown with model systems that biomolecule interactions might be highly sensitive to variations of contact duration within the subsecond range.
The architectures and the properties of the sugar-binding sites of HA33/C and HA33/A were shown to be drastically different.
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CEO of Professional Science Editing for Scientists @ prosciediting.com