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In order to identify specifically binding proteins, we generated biotinylated LTSM-positive probes from RPL36 and performed a protein pull-down from nuclear extracts in the presence of the unlabeled LTSM-negative RPS6 25mer competitor.
In order to determine whether expanded G4C2 transcripts might be toxic and sequester RNA binding proteins, we generated G4C2 with 8 ×, 38 ×, and 72 × repeats and expressed them in cell lines, primary neurons, and zebrafish embryos.
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To investigate how much the Pat-C conserved and basic patches contribute to RNA and protein binding, we generated three mutants.
We recognize that these mutations might also exhibit impaired interactions with other integrin binding proteins, and therefore we generated a number of mutants to reveal a general picture of the functional role of skelemin integrin interactions.
By combining an α-helical peptide that self-assembles into a hexameric coiled-coil bundle and an Fc-binding Protein A fragment, we generated the Hex nanocarrier that is efficiently internalized by cells without cytotoxicity.
To identify molecular specificity determinants that mediate dsRNA binding, we generated a RNA binding footprint based on a set of protein−RNA interaction persistence times.
FREX can in principle be applied to many binding proteins to generate a consistent ligand-dependent conformational change.
In addition, 21 unigenes were identified to encode long-chain acyl-CoA synthetases (LACS), and four unigenes encoded acyl-CoA binding proteins (ACBP), generating the ER acyl-CoA pool.
Using computational protein design, we generated mutants of the Ras-binding domain of Raf kinase (Raf) that stabilize the complex with RasGDP.
In the present work, we grafted a special red FP into three different location of a copper(I) binding protein, and generate a series of red fluorescent copper(I) sensors.
Figure 2A depicts an in vitro model of oxidative folding in which insertion of the correct disulfide pairings into reduced riboflavin binding protein (RfBP) generates an apoprotein capable of rapid and stoichiometric binding of riboflavin with complete quenching of the strong fluorescence of the free vitamin.
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