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The results obtained on the solution of several artificially generated test cases show a speedup of up to ∼12× with respect to the standard DD, depending on the interface size, the initial distribution and the number of parallel processes engaged.
ANN is also used for the solution of the inverse problem to determine the interface, size and location of delaminations using changes in measured natural frequencies before and after damage.
Once this treatment is achieved, it is possible to estimate compositions of phases and interface, size distribution of Si-nc, and particle density in the analyzed volume.
Based on this we can conclude that average interface size and the average number of interfaces residues/atoms between two macromolecules (DNA, protein) in any kind of complex (protein∶protein, protein∶DNA, protein∶protein∶DNA) are approximately the same.
Interestingly, although the interface size of SP4206 and IL-2 is only half as large as that between IL-2Rα and IL-2, SP4206 and IL-2Rα bind to IL-2 with similar affinities.
Relatedly, how easily does orthologous neofunctionalization occur and how dependent upon protein fold and binding interface size is it?
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First, we compared the interface sizes of fusion pairs versus nonfusion pairs.
Also increasing the cutoff further would make the ICs dependent on the protein sizes as more contacts will be detected for larger proteins, even at similar interface sizes.
In an extensive study by Marsh et al., 23 out of 27 heteromeric protein complexes showed excellent agreement between solution disassembly and interface sizes.
We hypothesize that, for these large complexes, the loss of some subunits may lead to tertiary and/or quaternary structural rearrangements, which could change the relative interface sizes.
We found excellent agreement between interface sizes and (dis)assembly, with seven out of nine complexes (23/27 total steps) agreeing perfectly with predictions (Table 1).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com