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Therefore, a mutation decreasing the pH threshold of the HA conformational change may affect the growth of H5N1 viruses in continuous cell lines.
This suggests that the C-terminal residue of the molecule is required for folding and was consistent with the tti2 suppressor mutation decreasing the proteolytic degradation of Tra1-F3744A and increasing its nuclear localization.
In this situation, any mutation decreasing the distance to the target is certainly fixed in the population, since the copies of the advantageous mutant retain the advantage of its progenitor.
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The mutation decreased the surrounding hydrophobicity and slightly altered secondary structure of the protein.
The K404E mutant is also suppressed by chloride but introduction of the K404E mutation decreased the chloride-dependence of E45K.
Molecular dynamic simulation studies indicated that the mutation decreased the subunit binding energy and modified the distribution of surface electrostatic potentials.
On the contrary, the T315I mutation decreased the flexibility of remote helix αI which suggests the synergistic effect between them.
This mutation decreased the sensitivity of the channel to barium block by 2.4 fold at −80 mV (Figure 8A).
The L41Q mutation decreases the Tm of Stx1B by 15°C, but Stx1B-L41Q remorestable sthane than Stx2B.
In agreement with an earlier observation [25], we found that the RAS2val19 mutation decreased the efficiency of G1 arrest during nutrient depletion (Fig. 1C and D).
Hence, our data therefore suggest that the R621C mutation decreases the capacity of the protein to form inclusions, which is consistent with data obtained in SH-SY5Y cells [24].
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