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Structure-based screens of interactions for specific molecular partners have been devised to accelerate protein interaction discovery, indirectly based on the premise that functional specificity of potential partners is also reflected by their phylogeny.
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Our methodological approach can easily be extended to other FG repeats, or mixtures of them, and thus provides a simple tool for the screening of interactions with NTRs in a relevant and well-controlled nano-environment.
High-throughput screening of interactions between over 20,000 metagenomic clones bearing large genomic inserts of culturable and noncultured bacteria and human cells have allowed the identification of several bioactive clones that modulate cellular activities with relevance to immune response, proliferation, or metabolism.
Also, because protein interaction data is derived by high-throughput screens of protein interactions in other cell systems, it is possible that unique protein interactions exist in the mammary gland have not yet been observed.
Thus a strategy that permits rapid screening of cell scaffold interactions is critical.
Building an ensemble of SWNT allows a partial screening of these interactions as revealed from the ohmic and non ohmic conductivity temperature and field dependencies.
Upon addition of NaCl or excess HCl a gel transformed back to a liquid resulted from the screening of electrostatic interactions.
Both the peak and slow mode disappeared by addition of NaCl or excess HCl into the solutions due to the screening of electrostatic interactions.
This work demonstrated that delivery systems may interact with the mucosal surface of intestinal cells, and in vitro approaches allow for screening of such interactions.
This paper describes a new analytical platform for the sensitive and selective screening of carbohydrate lectin interactions using plasmon waveguide resonance.
Optimization of the surface architecture through the introduction of an oligo ethylene glycol) spacer between the plasmonic surface and the glycan ligands provided an interface which allowed screening of glycan lectin interactions in a highly selective manner.
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