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Mutation of glycine to alanine destabilized the protein.
The breakthrough viral strain was DNA sequenced and shown to contain a substitution mutation of glycine to arginine at HBsAg aa position 145 (Gly/Arg 145) (145).
In contrast, the mutation of glycine at position 400 to valine (G400V) did not result in the reduction of enzymatic activity.
The mutation of glycine to an arginine in the P1′ position leads to an approximately 8-fold higher activity, whereas mutation of glycine to arginine at the P1 position yields a poor substrate, as does substitution of arginine for both glycine residues.
At position 368, two different codons (GCC or GCT) encode alanine suggesting either that the mutation of glycine to alanine originated from two independent events or that the C/T transition occurred in the GCC allele.
Finally, the mutation of glycine (618) to alanine would result in the formation of a side chain (although not so voluminous), which may have the potential of making further van der Waals interactions).
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The majority of these mutations are missense mutations of glycine residues occurring in the collagenous domain (Fig. 1).
RNA-sequencing showed that only LOC_Os08g07760 and LOC_Os08g08000 were expressed in young panicles, furthermore, only the SNP2 in LOC_Os08g07760 led to a nonsynonymous mutation of a glycine (GGT) to an aspartic acid (GAT) (Additional file 1: Table S2).
Mutation of this glycine to valine totally abolished the energy-transducing NDH-1 activity.
Mutation of a glycine at the top of the channel to a charged amino acid also reduces fatty acid inhibition.
Consistent with our earlier results we were unable to see any effect of mutation of individual glycine on the FAM150A-ALK interaction.
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