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On the basis of our data and the X-ray crystal structure of HGD, we present a structural model of MAC in a complex with HGD.
We present a structural model of human CRM1 based on a combination of X-ray crystallography, homology modeling, and electron microscopy.
Here, we present a structural model of YidC based on evolutionary co-variation analysis, lipid-versus-protein-exposure and molecular dynamics simulations.
Here we present a structural model of tandem IgC2 domains of skelemin in complex with the cytoplasmic tails of integrin αIIbβ3.
In this study we define the catalytic G-domain interface by mutagenesis and present a structural model, of how GTP hydrolysis is activated in Irga6 complexes, based on the substrate-twinning reaction mechanism of the signal recognition particle (SRP) and its receptor (SRα).
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We show that several residues conserved across cathepsin L sub-family proteases are necessary for this inhibition, and present a structural model for the interaction of the falcipain-2 prodomain with both its own mature domain and that of other proteases.
Based on the two structures above, we presented a structural model of Dpy30C in complex with its target helix in a 2 1 ratio, as shown in Fig. 1G.
Overall, this work presenting a structural model of the active ribosome-bound FoC YidC complex will have a significant impact within the YidC field and the membrane field in general.
We go on to present a structural model in which KBU2046 binds within a cleft that is created through the binding of HSP90 and CDC37, and exists at the interface between these two proteins.
The results are graphically presented on a structural model of CXCR4.
In cases where the structure was of a homologous protein (e-value < 1E-20) and where most of the interface residues were present, we generated a structural model of the target protein using comparative modeling.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com