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Distance measurements to carbons are performed using a 2D transferred echo double resonance (TEDOR MASsolid-statete NMR experiment, and water binding is probed by heteronuclear high-resolution proton-lithium and proton-carbon correlation (wPMLG-HETCOR) experiments.
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With baseline exchange for both wild type and the T315I proteins, inhibitor binding was probed by HX MS. Each inhibitor was first incubated individually with wild-type Abl or T315I and regions with differences in HX were observed.
Anion-binding studies in solution: Anion binding was probed by using NMR, luminescence and electrochemical methods in assorted solvents as dictated by various factors.
The binding mechanism is probed by comparing their results to coordinating phosphorylated mono- and triethylene glycol diethyl esters (pEG1 and pEG3) and the diprotic phosphonic acid (DPA) that operates by ion exchange.
The kinetic adsorption profile at the DNA gold nanoparticle (AuNP) interface is probed by following the binding and organization of thiolated linear DNA and aptamers of varying chain lengths (15, 30, 44, and 51 mer) to the surface of AuNPs (13.0 ± 1.0 nm diameter).
The morphology was examined by TEM and SEM and the binding interactions were probed by FITR spectroscopy.
Putative hydrophobic ligand binding in solution was probed by comparison of ANS (ca. 10 µM) fluorescence emission (390 nm excitation) in the presence and absence of rlatherin.
hRNase3 binding to lipids was probed by primary antibody (mouse anti-6His 1 : 5000) for 1 h.
The binding of these antibodies was probed by fluorescent dye-conjugated secondary antibodies.
The relative contributions to binding of these residues were probed by mutagenesis in CpOGA.
The binding of HMGB1 peptide was probed by HRP-conjugated streptavidin.
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