If tRNA-ribosome contact sites were lost or mutated in the ribosome, it would have allowed the tRNA genes to accrue mutations at these contact sites.
Mutations at these sites can both increase and decrease ADP inhibition.
In contrast, phospho-deficient mutations at these sites led to inactivation of eNOS.
Whilst the introduction of mutations at these sites negated favourable characteristics such as thermostability, several favourable effects were observed.
Mutations at these locations took place only relatively late in the anthropoid lineage leading to humans and apes but not in the strepsirrhine lineage leading to O. garnettii.
We assayed the enzymatic activities of proteins carrying different mutations at these sites, providing more clues for screening drugs regulating the activity of DGAT1.
Mutations at these sites, by altering the relationship between force and calcium, may provide significant insights into the molecular mechanisms controlling the energetics of positive inotropy.
Further genomic PCR of 2 NPG-specific mutant gene sites Il2rg and Prkdc showed that both the 2 NPG ESC lines possessed NPG specific mutations at these sites (Fig. S1).
The ARG residues at positions 4 and 9 are significantly less positive than the rest of the ARG residues, indicating that mutations at these positions may be less effective.
In the computational complex model, the sidechains of these residues do not form key interactions with TACE, but experimentally, the mutations at these two positions largely affect the peptide cleavage efficiency in the enzymatic assay.
For example, Pol η mediates error-free bypass of lesions induced by UV irradiation, whereas Pol ι introduces mutations at these sites.
