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Kinase substrates are difficult to identify because of the large size of the kinase superfamily (over 500 human kinases) and the large number of low-abundance substrates that kinases are predicted to phosphorylate.
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It should be noted that the lipid bilayers on the substrate are difficult to control, even under the same protocol and conditions.
The value of the bias on the surface of a dielectric substrate is difficult to monitor during plasma processing.
Docking study shows that few amino acids of active site of enzyme are also involved in meropenem binding, hence substrate is difficult to bind on active site properly and does not get hydrolysed.
A study of the kinetics of the conversion of this substrate was difficult, however, since only low substrate concentrations (maximal 26 µM) could be used in the assay and thus saturation of the enzyme could not be achieved.
Short chain dehydrogenases catalyse a wide range of functions so the precise function and identity of the substrate is difficult to deduce from sequence alone.
Given the reactivity of both molecules, however, the ability of either to act as a RebC substrate is difficult to test directly (5).
Also, the less pronounced increase in LFD resulting from enzymatic hydrolysis of the OPHS-D substrate is difficult to explain, unless drying and rewetting would decrease the extent of longitudinally distributed non-crystalline regions.
Copper is one of the substrates that are difficult to coat with a diamond-like carbon film because of the latter's poor adhesion.
Moreover, acetyl-CoA is native to E. coli in large amounts, whereas branched-chain substrates for FabHB are difficult to accumulate in E. coli [ 46, 55].
SUMO substrates are often difficult to validate due to the low stoichiometry of the SUMO modification: however, proteomic approaches have lead to the identification of many putative substrates (reviewed in Rosas-Acosta et al., 2005).
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