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Unlike nucleoside RTIs, which bind at the enzyme's active site, NNRTIs bind allosterically at a distinct site away from the active site termed the NNRTI pocket.
Unlike nucleoside reverse-transcriptase inhibitors, which bind at the enzyme's active site, nevirapine binds allosterically at a distinct site away from the active site termed the non-nucleoside reverse transcriptase inhibitor pocket.
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Analysis of the deposited 3D structures of the kinetically evaluated enzymes complexed to the phosphate-based inhibitors indicate that malonate could be a good phosphate surrogate only if phosphate is not tightly bound at the enzyme active site, such as in position 7 of compound 1 for FBAs.
Although ATA is structurally distinct from sialic acid, molecular modeling experiments suggested that ATA binds to NA at the enzyme's substrate binding site.
In a non-competitive-type of inhibition, both the inhibitor and substrate can bind to the enzyme at the same time because they have separate binding sites on the enzyme, and therefore, the substrate or inhibitor does not affect the binding of the other to the enzyme.
In mixed inhibition, the inhibitor can bind to the enzyme at the same time as the enzyme's substrate.
competitive inhibitor and substrate cannot bind to the enzyme at the same time.
In these enzymes, both substrates bind to the enzyme at the same time to produce an EAB ternary complex.
In competitive inhibition, the substrate and inhibitor cannot bind to the enzyme at the same time, as shown in the figure on the left.
Serendipitously, Ches was found bound to NanB at the enzyme active site, and was found to inhibit NanB with a Ki of ∼ 0.5 mM.
Structure-based inhibitor design has led to the discovery of a number of potent inhibitors of glycogen phosphorylase b (GPb), N-acyl derivatives of β-d-glucopyranosylamine, that bind at the catalytic site of the enzyme.
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CEO of Professional Science Editing for Scientists @ prosciediting.com