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These data support the use of low-temperature culture conditions under induction by DOX to increase protein production without eliminating the binding activity and structural integrity of the protein of interest.
(2) Amidases produced by S. aureus wild type bacteria would shave and remove the most accessible PGN fragments at the surface of bacteria, eliminating the binding sites for PGRPs.
However, the atl mutant would release intact muropeptides, easily detected by PGRP-SA, and therefore would be unable to evade detection by the innate immune system; Hypothesis 2: S. aureus wild type bacteria shave and remove accessible PGN fragments at the surface of bacteria, eliminating the binding sites for PGRPs.
Dr James Faeder This paper presents a simple mathematical model to describe the spatial distribution of drug in tissue where the drug may interact with another molecule (e.g. protein) to form a complex that undergoes degradation at a different rate from the drug alone, producing back again the active drug and eliminating the binding partner.
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Mutating the first P in the human PXXXPR motif (P309V) eliminated the binding of hTTP to CIN85 (Fig. 4E3, lane).
Moreover, changing the first proline in this motif to valine (P309V) in hTTP eliminated the binding of hTTP to CIN85.
This speculation is also supported by the results from our control experiment, in which excess CIDR reduces but not eliminate the binding between CD36 and IRBCs.
A 10, 25, and 100-fold molar excess of XRE-I motif gradually eliminated the binding of AhR to the XRE-like motif (Fig. 8, Lane 1 4); by contrast, appreciable complex of AhR to the XRE-I sequence remained even at a 100-fold molar excess of the XRE-like sequence (Fig. 8, lanes 5 8), consistent with stronger AhR binding to XRE-I than to the XRE-like sequence.
We found that removal of five or eight C-terminal amino acids had no effect on CIN85 binding (Fig. 4A2, lanes 4 6); however, removal of either 14 (aa 1 313, Fig. 4A2, lane 3) or 37 (aa 1 290, Fig. 4A2, lane 2) C-terminal amino acids in hTTP, in both cases removing the PXXXPR motif, completely eliminated the binding, suggesting that this PXXXPR motif is critical for forming the complex with CIN85.
On the other hand, deletion of the center domain of ZBTB16 eliminated the binding to Atg14L.
Can they eliminate the binding of oleic acid with precise point mutations?
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