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The increased dynamics of hPCNA relative to scPCNA may allow it to acquire multiple induced conformations upon binding to its substrates enlarging its binding diversity.
After binding to its substrates, Pin1 can facilitate the cis-trans isomerization of pSP/pTP peptidyl-prolyl bonds through its PPIase domain, resulting in conformational and functional changes of substrate proteins.
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Inhibitors can be used to stop an enzyme from binding to its substrate.
Similar to the observations from ubiquitin, the lysozyme landscape is also composed of sub-states that share common structural features which have direct relevance in binding to its substrate.
Thus, these data argue that the two neighboring r-proteins, namely the platform component rpS14 and the head component rpS5 contribute to a local environment in the head-platform cleft around the SSU rRNA 3' end which is not required for Nob1p binding to its substrate, but to efficiently trigger pre-rRNA cleavage by Nob1p.
Additionally, Merlin has also been shown to function in nuclei by inhibiting the activity of the nuclear E3 ubiquitin ligase CRL4DCAF1 via binding to its substrate adaptor DCAF1.
At low concentrations of NAD+, integrin α7 is modified exclusively within the stalk region of the molecule, leading to an increased binding to its substrate laminin.
Divalent cations affect integrins affinity and specificity; a balance between calcium, zinc, magnesium, and manganese may modulate integrin binding to its substrate [ 14– 17].
Within the cell, 11β-HSD2 is localised to the endoplasmic reticulum, with a cytosol-facing active site and co-factor binding domain, and binds to its substrate with around 100-fold more affinity than 11β-HSD1, suggestitg it may play a more dominant role in corticosteroid metabolism in tissues if the two enzymes are co-expressed [65].
Here, we increase the regulatory range of the Rnt1p control elements, by modifying a critical region for enzyme binding to its hairpin substrates, the binding stability box (BSB).
Multi-drug resistant (MDR) 769 HIV-1 protease (resistant mutations at residues 10, 36, 46, 54, 62, 63, 71, 82, 84, 90) was selected for the present study to understand the binding to its natural substrates.
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