Single channel analysis of T142S revealed that the T142S mutation had minimal effects on single channel conductance or sensitivity to permeant ion concentrations (Figure 7C F) but caused a marked change in the single channel gating properties (Figure 7G).
In contrast, the P12T mutation had minimal effects on the tet(V) promoter.
It is also interesting to note that while the A2′S mutation had minimal effect on receptor function, the A2′T mutation abolished glutamate-induced currents.
Riggs et al. [ 17] reported that the P124S mutation had minimal effects upon the observed transcription levels of FKBP52 whether introduced into wild-type FKBP52 or into the P119L background.
It was reported that dgat or pdat mutation had minimal impact on oil content in Arabidopsis seeds, showing that the overlapping functions of PDAT and DGAT are essential for TAG biosynthesis [ 62].
This confirms that the introduction of these mutations has minimal impact on the knockin animals compared with controls, minimizing the risk that effects unrelated to the behavior being investigated confound the results.
Electrophysiological measurements show that drug-resistant mutations have minimal effects on M2's specific activity, and suggest that resistance is achieved by altering a binding site within the pore rather than a less direct allosteric mechanism.
These data, together with the observation that HCV E2 protein bound mutant and parental CD81 with comparable values, suggest that the mutations have minimal effect on CD81 conformation.
However, despite the disruptive phenotypes observed in homotetrameric Thr441Val or Thr442Val channels, single subunit mutations had minimal effects in the background of a concatenated tetramer.
While gankyrin mutation K116A and double mutation D39A/D71A had minimal effects on binding affinity (Table 1, entries 9 and 10, respectively), an R41A mutation significantly decreased affinity [ KD = 313.3 ± 17.6 nM (Table 1, entry 8)].
