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FAST-NMR combines NMR ligand affinity screening [22] using a fragment-based functional library [23] with structural biology and bioinformatics [8] to rapidly determine protein-ligand complexes [24] and infer functional relationship between proteins based on similarities in functional epitopes.
We have developed and applied immunization and affinity screening methods to develop a primary library of recombinant single chain variable fragment (scFv) antibodies in an M13 vector, pKM19.
To support the current needs, Sierra Sensors introduced a surface plasmon resonance imaging (SPRi) based biosensor, Molecular Affinity Screening System (MASS-1).
Rice GT-2 and tobacco GT1a/B2F were the first two nuclear proteins identified via affinity screening using GT2 sequence and Box II sequence [24] [26].
The two mimotopes of urease B were characterised via affinity screening, binding, competitive inhibition and DNA sequencing.
The fast affinity screening results included the discovery of a lipid phosphatase inhibitor involved in type 2 diabetes [ 64].
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These libraries can be affinity-screened via the protein moiety (phenotype) followed by decoding of the nucleic acid moiety (genotype) to identify the selected proteins.
A structural and functional relationship between the bacterial T3SS and eukaryotic apoptosis was identified using our FAST-NMR ligand affinity screen in combination with a bioinformatic analysis based on our CPASS program.
A structural and functional similarity between PrgI, a type three secretion system protein, and Bcl-xL, a member of the Bcl-2 family of proteins involved in eukaryotic apoptosis, was identified from a FAST-NMR ligand affinity screen in combination with a bioinformatic analysis.
A high-throughput NMR ligand affinity screen was performed with a function-based compound library.
Confirmatory assay was based on a surrogate affinity screen using the same principle as the primary assay.
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