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We show that in all but one protein (AcP) folding nucleus residues are significantly more conserved than the rest of the protein.
This approach is based on the observation that protein structures are significantly more conserved in evolution than linear sequences, and mechanistic similarities among diverse transporters are emerging.
The motif copies are significantly more conserved than the surrounding sequence, which suggests that they play an important functional role.
Despite this inter-serotype variability, the P1-P2 sequence of 5'NCR was significantly more conserved between clinical isolates and the corresponding reference prototype strain (mean divergence 3.5%) compared to the NIm-1A coding sequences of VP1 (mean divergence 9.6%, Table 1).
In addition, tele-enhancers are significantly more conserved than their proximal counterparts.
Transmembrane domains were significantly more conserved than either intracellular or extracellular domains.
The HH region was significantly more conserved than the non-hammerhead (NHH) region of the pDo500 repeat.
ConsWin works well on our enzyme dataset, because residues in enzyme active sites are significantly more conserved than the background.
In particular, it is observed that the network peripheral domains are significantly more conserved than the core domains.
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As shown in Fig 2 (a, b), polymorphism mutation sites are significantly biased towards less conserved sites while disease mutation sites are significantly biased towards more conserved sites (p-values < 10-5 in both cases).
However, the number of sampled yeasts and Basidiomycota are very small so that only 5′SSs of yeast RIs are significantly more highly conserved than 5′SSs of basidiomycetous RIs (P = 0.036, n = 2 yeasts (yeast P. stipitis contributes no RIs), 5 Basidiomycota).
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