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As Figure 10 illustrates, there is great diversity in the relative performance of the benchmark enzymes depending upon which hydrolysis mode and protein assay basis are examined.
To estimate the relation between evolution mode (for example, positive selection mode) and protein function, the permutation statistical test was used.
The main difference between the two modes of cross-validation is that the train-test split is based on proteins in the first mode and protein pairs in the second mode.
However in attaining high conversion yields at lower total enzyme protein loadings, the relative and rank ordered performance of the enzyme systems varied significantly depending upon which hydrolysis mode and protein assay were used as the basis for comparison.
One of the enzyme preparations ('enzyme B') exhibited the best absolute performance in terms of attaining high conversion yields at lower enzyme loadings under all conditions tested, but the relative performance of the four enzyme systems to one another varied significantly depending upon which hydrolysis mode and protein assay were used as bases for comparison.
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Here we introduce methodology to calculate protein normal modes and protein molecular dynamics in torsion space which enable the development of multiple protein states to address the natural flexibility of proteins.
Five peptides were sequenced in MSMS mode and the protein identified corresponds to a protein of 161 amino acids, FLJ20625 (Figure 1A).
One-mode projections, when only core proteins or only attachment proteins are considered, are shown to have exponential degree and strength distributions for both complex-mode and protein-mode projections, similar to the case without the distinction between those two kinds of proteins.
Buttons of the first row show the DNA in surface mode and the protein in balls-and-sticks mode, thus focusing on the protein side of the interface.
A unique advantage of HIC is that it is a very mild method for high-resolution protein separation in a nondenaturing mode and preserves proteins' tertiary structure and biological activity.
In order to predict the binding mode between ATX and protein kinase Cδ (PKCδ) C1B domain, we carried out molecular docking simulation, atomistic molecular dynamics simulation in phospholipid membrane environment, and structure activity study on a simple acyclic analog of ATX.
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