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Fragment-based approaches are used routinely to discover enzyme inhibitors as cellular tools and potential therapeutic agents.
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Current methods to study protein structure are very interesting to discover enzymes with improved catalytic properties and activities [ 19].
Hence, we can leverage a naturally evolved physiological characteristic of an enzyme and use it as a proxy to discover enzymes with a non-natural industrially relevant characteristic, such as IL-tolerance.
This system is quite different from the previously characterized termite fermentation system and provides new opportunities to discover enzymes that could be exploited for cellulosic ethanol biofuel production or the development of novel methods to control wood-boring pests.
Labour-saving aside, functional metagenomics is also powerful, because it holds the potential to discover enzymes whose sequences are hitherto unknown [ 16], an attribute that is particularly welcome in the light of the recent discovery that CAZy family 33 carbohydrate binding modules are actually oxidative enzymes that facilitate the action of glycoside hydrolases [ 17].
The newly discovered enzyme acts upon histones, the specialized proteins that strands of DNA loop around.
Tyrosyl DNA phosphodiesterase 2 (TDP2), a newly discovered enzyme that cleaves 5′-phosphotyrosyl bonds, is a potential target for chemotherapy.
The newly discovered enzyme shows potential for application in CCUS owing to its acceptable catalytic activity and extremely high thermostability that are desirable attributes for CO2 biomineralization.
Establishing a reliable initial-rate assay for a newly discovered enzyme also presents the opportunity to uncover new catalytic and regulatory properties.
Nitrile reductase is a newly discovered enzyme class that can catalyze the reduction of nitriles directly to amines, a very important reaction in synthetic organic chemistry.
In order to add this side chain to acyl ghrelin, it is necessary for the recently discovered enzyme, ghrelin-O-acyl transferase (GOAT).
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