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FruA-His6 alone failed to produce a distinct complex, but in combination with His10-MrpC2, a slow-migrating complex es) was produced more abundantly than could be accounted for by binding of each protein alone, suggestive of cooperative binding.
When His10-MrpC2 waddedded, a slow-migrating complex es) was produced more abundantly than could be accounted for by binding of each protein alone, providing evidence for cooperative binding.
It inhibits bacterial protein synthesis by binding of each component to a different site on the 50S subunit of the bacterial ribosome, dalfopristin leading to a conformational change in the ribosome which increases the affinity of the ribosome for quinupristin.
The combination of FruA-His6 and His10-MrpC2 produced a slow-migrating complex es) more abundantly than could be accounted for by binding of each protein alone, providing evidence for cooperative binding.
In EMSAs, cooperative binding produced a slow-migrating complex more abundantly than could be accounted for by binding of each protein alone [ 46], and similar results provide evidence for cooperative binding of the two proteins in the fmgBC [ 47], fmgD [ 45], fmgE [ 48], and dev [ 53] promoter regions.
Addition of a 10-fold lower concentration of His10-MrpC2 thethe 2-fold lower concentration of FruA-His6 produced slightly more complex than could be accounted for by binding of each protein alone, consistent with cooperative binding, but surprisingly a novel, slow-migrating complex was observed only for the MXAN_6247 region.
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EGF family receptors are directly regulated by binding of diverse polypeptide hormones that each contain a 6-kDa domain that is homologous to EGF (for review [ 19*, 20*, 21*]).
Based on the crystal structure of classical cadherins (Boggon et al. 2002; Overduin et al. 1995; Shapiro et al. 1995), the EC 1 4 domains are thought to be connected via flexible linkers which are rigidified by binding of up to three Ca2+ ions each (Pertz et al. 1999).
Activation of each Trk receptor is triggered by binding of the cognate neurotrophin at highly specific contact regions.
LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins.
Initial binding of the coenzyme NADH to the subunit was followed by binding of pyruvate (Fig. 4A).
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