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The working principle of the biosensor relied on the enzymatic reaction of AA on starch and GD on the generated maltose, as in (7) and (8), respectively.
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The use of biosensors relies on the assumption that their activity is linearly proportional to the activity of the signaling protein they have been engineered to track.
Biosensors relying on the fluorescence resonance energy transfer (FRET) between fluorescent proteins have been used for live-cell imaging of cellular events including Ca2+ signaling.
Reagentless biosensors rely on the interaction of a binding partner and its target to generate a change in fluorescent signal using an environment-sensitive fluorophore or Förster resonance energy transfer.
In a nutshell, the idea behind the nanopore-based biosensors relies on the fact that the single macromolecule capture, and subsequent interactions of the molecules and the pore, produces a displacement of electrolytes in the channel, leading to a sudden decrease in conductivity which can be resolved and recorded using low noise feedback-loop operational amplifiers.
The SPR biosensors rely on this property of the resonance.
Both glycoproteins could be detected down to 150 fM level with a possibility to see microheterogeneity of glycan composition on fetuin by the biosensor relying on determination of changes in the RCT.
The design of the biosensor relies on a large conformational change of ParM that occurs on nucleotide binding: the two subdomains of the actinfold rotate against each other by 25°, thereby closing the nucleotide-binding site located in a cleft between them [ 13].
The specificity of DNA biosensors relies on single-stranded oligonucleotide probes immobilized to a transduction platform.
Construction of reagentless fluorescent biosensors relies on identification of sites that undergo a local conformational change in concert with the global, ligand-mediated hinge-bending motion.
Many applications for medical therapy, biotechnology and biosensors rely on efficient delivery and release of active substances.
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