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Molecular dynamics simulation for KdsA and KdsA-4636 complex was performed for 100 ns to unveil what conformational changes the enzyme underwent in the absence and presence of the inhibitor, respectively.
Chemical nano-immobilization method changes the enzyme conformation, but it provides the strong covalent bond formation.
In such mechanisms, substrate A binds, changes the enzyme to E by, for example, transferring a chemical group to the active site, and is then released.
This usually changes the enzyme activity, cellular localization, or interaction with partners of the target protein (Hanks and Hunter 1995).
These two alleles differ at two sites, resulting in two amino acid changes: the enzyme encoded by ADH1C*1 (γ1-ADH) hArgatg at position 272 and isoleucin (Ile) at position 350, whereas that encoded by ADH1C*2 (γ2-ADH) has glutamine (Gln) at position 272 and valine (Val) at position 350 (Osier et al. 2002).
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With some changes, the enzyme-producing bacteria might also prove effective in the detection of other cancers of the gastrointestinal tract, such as colorectal cancer.
The Gln11Met mutation, which converts the signature glycine motif in PfMDH to that of PfLDH, did not change the enzyme function.
We subjected residue 342 to saturation mutagenesis, and further changed the enzyme by random mutagenesis and two rounds of DNA shuffling.
Results showed that N addition did not change the enzyme ratio (1 1 1) of C, N, and phosphorus (P) acquisition, and also did not change vector angle of ecoenzymatic stoichiometry which is an indicator of microbial P limitation.
For the reduction of phenylglyoxylic acid, the immobilization process changed the enzyme's optimum temperature from 30 to 40 °C, the enzyme's optimum pH from 6.8 to 6.0, and the immobilized SCAD retained 62.76% of its original activity.
Starting from the X-ray structure of the mutated enzyme-substrate complex we changed the enzyme into the active form to reach the reactant state.
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