Sentence examples for mutating the arginine from inspiring English sources

R304A and R304K point mutants of PLD1 were generated by mutating the arginine residue at 304 to Ala or Lys respectively.

In summary, mutating the arginine finger motif of AAA4 confers motile properties similar to those produced by Lis1; moreover, the same mutation can in part circumvent the requirement for Lis1 in A. nidulans (Zhuang et al., 2007).

For example, we mutated the arginine residues in the hub cavity that we have implicated in the exchange process, but this resulted in a substantial loss of fluorophore labeling at residue 335, indicating that the structure of the hub domain might be compromised.

To investigate potential roles of these arginine residues in ATP hydrolysis we mutated each to methionine and compared them with effects of mutating the predicted arginine fingers R334 (NBD1) and R765 (NeuwaldNetwald et al., 1999).

Furthermore, mutating the methylated arginine residues on PGL-1 and PGL-3 resulted in impaired degradation of PGL-1 and PGL-3 [ 145].

By mutating the target arginine on NF-κB to a lysine residue and therein blocking the ability of PRMT5 to methylate NF-κB, a more dramatic dysregulation of gene regulation was observed than by knocking down PRMT5.

Interestingly, although mutating the two arginines increases overall remodeling rates, the rates remain sensitive to the presence of the H4 tail basic patch.

To determine whether the proposed NLS of Atx3 was indeed responsible for the translocation of the fusion protein into the nucleus of yeast cells, we mutated the conserved arginine residue within the putative NLS sequence into a threonine residue pNIA-GFP-Atx3R282T pNIA-GFP-Atx3R282T pNIA-GFP-Atx3R282T

A subsequent in vitro experiment demonstrated a significant loss of bioactivity upon mutating the terminal residue from arginine to lysine, thereby corroborating the overall findings of the computational model.

To begin to determine the role of the catalytic activity of CYK-4 during cytokinesis, we first studied the consequence of mutating the highly conserved catalytic arginine that stabilizes the transition state during GTP hydrolysis.

A total of 21 of these mutations affected residue 282, mutating this arginine to either cysteine or histidine.