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The structure demonstrates the catalytic mechanisms of both enzymes and reveals the structural basis of mutations causing Schindler and Fabry diseases.
In addition, mapping disease-causing mutations to the structure demonstrates clear correlation between severity of disease and mutation location.
Interestingly, the structure demonstrates that extensive intramolecular interactions take place between the RING domain and the C2HC ZnF (Fig. 7A).
The structure demonstrates the robustness and versatility of GCN4 as a fusion adaptor.
The structure demonstrates that for steric reasons, homodimeric IL-5 can bind only one receptor molecule, even though two equivalent receptor-binding sites exist.
The structure demonstrates that the actin dimer in the complex does not represent a physiologically relevant entity, for the two actin molecules do not interact with each other.
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Illustrations of the structure demonstrate how the resulting classifications avert double counting and other ambiguities.
The structure demonstrated a central role for SEPT2 in filament formation, and definitively established that septins, as opposed to actin and microtubules, form non-polar filaments.
We assessed the mathematical fit of any graphical structure (i.e., pattern) observed, how this fit scaled between group and individual data, and whether the structure demonstrated the signature of a power law.
The structure demonstrated that the Ana2 CCCD forms a parallel, symmetrical 4-helix bundle, with a left-handed supercoil.
Determination of the structures demonstrates that a unique hydrogen-bonding network and the sulfur atom of the chromophore are critical to the photoswitching property of Dronpa.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com