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The rotation of this glutamate into salt-bridging distance with a lysine moiety correlates with an enhanced enthalpic contribution to binding for these highly potent thrombin binders.
Thermodynamics of the binding from isothermal titration calorimetry experiments revealed an entropy driven binding for these analogs compared to the enthalpy driven binding of berberine.
The long retention of these ligands in the normal mouse brain suggests that there may be high binding for these probes in the brain not associated with Aβ plaques.
Moreover, the degree of micellar counterion binding for these surfactants was determined by using a bromide ion-selective electrode, which indicated relatively high values (0.8 0.9) for Cn-2Am (n = 18, 20, and 22) and more common values (0.5 0.8) for Cn-3Am (n = 18, 20, and 22).
However, there are differences in the mode of binding for these glycans to the various HAs.
The ligand-receptor binding for these four genes can not be determined in this study.
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It should be noted that the MyTH4 FERM cassette may possess uncovered binding sites for these binding partners or that these bind other domains of myosin-X.
In addition, the selectivity between SGTP- and GTP-binding for these SGTP targets was further characterized.
Therefore, our SGTP affinity profiling assay and SGTP/GTP competition assay could allow for site-specific determination of the SGTP binding affinity and selectivity toward the unique P-loop motif sequence, which is known to be directly involved in GTP-binding for these GTPases.
Neuro2A cells might over-express certain gene(s) that contain(s) multiple binding sites for these RNA-binding molecules, leading to the assembly of CS bodies, most likely at the transcriptional site.
Molecular docking simulations were carried out and these studies suggested a different binding orientation inside the CDK2 binding pocket for these analogues compared to flavopiridol.
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