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When running STAP on a TF dataset from ChIP-chip or ChIP-seq experiments, we generally need to use only a subset of data for training the binding model, while the rest can be used as testing data.
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The FP measurements indicate that MrkH binds the longer mrkA regulatory fragment (from −117 to +166) with a K d value of 3.07 μmol/L using the one site specific binding model, while MrkH binds to a shorter mrkA regulatory fragment (from −117 to −37) with a K d value of 8.24 μmol/L.
We therefore analyzed the data using a more sophisticated approach; the R3 (nonspecific) binding data were fit to the nonspecific finite lattice DNA binding model (eq 3a), while the I1 (cos-specific) binding data were simultaneously fit to the competitive specific/nonspecific finite lattice DNA binding model (eq 3b).
This approach results in an excellent fit to both data sets; the monotonic interaction of IHF with nonspecific DNA is described well by the nonspecific finite lattice DNA binding model (black line), while the competitive specific/nonspecific finite lattice DNA binding model captures the biphasic transition of specific plus superimposed nonspecific binding events (solid red line).
Molecular docking of 4g into S. aureus Enoyl-ACP-reductase active site were performed to determine the probable binding mode, while the QSAR model was built to check the previous work as well as to introduce new directions.
Thermodynamic data were analyzed with a single-site binding model using MicroCal PEAQ-ITC Analysis Software provided by the manufacturer.
Plus, a hydroxyl-dependent chloride binding model is established to quantify the distance-associated chloride binding capacity.
The following section describes the Hitch Hiker binding model.
Molecular graphics for the best binding model was generated using Discovery Studio Visualizer 2.0.
The corresponding tight binding model is also constructed.
CSP titration curves were fitted using the one-site binding model.
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