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The possibility that an unrecognized more complex enzyme organization near the nucleus may exist is a stimulating proposal worthy to be investigated.
Also, descriptions of more complex enzyme mechanisms contain numerous parameters if several substrates or reactions are involved, so that the alleged functions cannot be identified from the typically sparse data [ 4, 5].
The stable MRM system is also capable of evolving more complex enzyme functions like that of a replicase or membrane synthesis – this leaves the possibility for MRM to evolve towards membrane-coated self-reproducing vesicles (protocells) open.
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More complex enzymes may not be correctly folded in an ectopic environment and, as a result, may be less efficient at converting the prodrug.
For similar reasons, most nucleic acid circuits have been implemented in vitro rather than in the much more complex (and enzyme ridden) environment of a cell.
We analytically illustrate how this simple dependence may be extended to more complex single-enzyme reactions, and experimentally verify the invariance to average enzyme levels using a β-galactosidase assay.
This suggests a more complex multi-enzyme system for K36 methylation in higher eukaryotes, similar to that for K4 methylation.
A more complex two-step enzyme reaction was designed by placing the membranes in a fluidic device at fast flow rates which affords short residence times even in second(s) are sufficient to get substrate transformation.
Results, therefore, pointed to a more complex substrate-to-enzyme reaction rate relationship for UG.
Most curves exhibited a more complex pattern with declining enzyme velocity at higher substrate concentrations (Supplementary Figure S7).
Though our studies demonstrate the proof of principle, they also suggest more complex interaction of both enzymes underlying the mechanism of their reciprocal regulation.
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