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Mutations at three positions were introduced to the XYNII mutant containing a disulfide bridge (S110C N154C) in the α-helix.
An hCaM mutant containing a unique cysteine residue at position 124 on the protein was expressed, purified, and chemically modified with the fluorophore monobromobimane (mBBr).
Here, we present a lipase mutant containing a biochemical switch allowing a controlled opening and closing of the lid independent of the environment.
Equilibrium binding studies of a RecBC mutant containing a nuclease domain deletion, RecBΔnucC, suggest that looping of the 3′-tail (when n ≥ 6 nucleotides) occurs even in the absence of the RecB nuclease domain, although the nuclease domain stabilizes such loop formation.
Surprisingly, the GAM-proghrelin mutant containing a Ser6 to Ala6 mutation was octanoylated, while the Ser5 to Ala5 mutant was not (Figure 7C, lanes 2 and 3).
This pattern was previously observed in cells expressing the inactive Gap1-92 mutant containing a single glutamate-to-lysine substitution at position 300 and shown by membrane fractionation to be stacked in the ER [4].
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These peptides have properties similar to apoA-I Milano [17], [43], a naturally occurring apoA-I mutant containing an extra cysteine disulfide bridge.
The construct pET28a MsrB1-Cys, described previously [22] was used for expression of MsrB1-Cys mutant containing an N-terminal His-tag in E. coli BL21 (DE3).
The main chlamydomonas strains exploited were IL, a mutant containing an intronless psbA gene [46] that represented the control reference strain for characterization of the D1 mutants, and Del1, a mutant used as a recipient strain for D1 mutants generation.
To determine whether the presence of cysteine residues is sufficient to allow for functional activation in the absence of tyrosine phosphorylation, we used a STAT1-CC mutant containing an Y701F substitution.
To investigate if this is so, we have conducted NMR studies of a Pin1 mutant containing an alanine substitution designed to weaken Pin1's capacity for interdomain contact.
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