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For a quick example, Fontes and Gilbert (2010) explained that calcium is pivotal for dockerin (a facet of most enzyme structures) stability and function, and in the presence of ethylenediaminetetraacetic acid (EDTA, a chelating agent), dockerins are unable to interact with cohesins (another facet of most enzyme structures).
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These knowledge-based studies greatly benefit from the most recent computational analyses of enzyme structures and functions.
Most of the enzyme structure has fixed three-dimensional conformation.
Within the analyzed group of inhibitors, analogously to the bacterial enzyme, structures 4 and 9 were the most potent with Ki values equal 21 and 3.7 μM, respectively.
It is the most common protein fold and is present in approximately 10% of all known enzyme structures.
BSX has a TIM-barrel structure, which is the most common folding pattern among protein catalysts and is present in approximately 10% of all known enzyme structures.
While the network structure and catalysed reactions are now fairly well established and can be extracted using the genome annotation, most enzyme kinetics are still unknown.
Like most enzymes, gamma-secretase is expected to move through several different three-dimensional shapes to perform its role, and identifying these structures could help us to understand how the enzyme works.
Most enzymes can be denatured that is, unfolded and inactivated by heating or chemical denaturants, which disrupt the three-dimensional structure of the protein.
Enzyme structure and function are routinely studied by altering the DNA that encodes the enzyme, thus replacing specific amino-acid residues in the enzyme with other residues.
Fersht, A. R. Enzyme Structure and Mechanism 2nd edn (Freeman, New York, 1985).
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