In contrast, the structure of the heme domain of the BM3 F393H mutant would not fully account for all of the properties of the F393H mutant protein even if the histidine were protonated.
In HeLa cell transfectants, wild-type DHODH showed a 5-fold increase in DHO-dependent enzymatic activity after induction; however, in the R135C mutant, there was no increase in DHO-dependent enzymatic activity after induction of the mutant protein, even if the protein expression increased 5-fold.
We also found that VCP associates with either wild-type or mutant ZIP13 proteins, even though it preferentially interacts with the mutant ZIP13, suggesting that the VCP ZIP13 interaction is important for both the normal steady-state turnover of wild-type ZIP13 and the clearance of ZIP13 proteins containing critical mutations (Fig 6).
The ER lumen has a remarkable ability to maintain homeostasis and any physiological or pathological stimuli that leads to an increase in misfolded proteins, such as alterations in re-dox balance and calcium concentrations, glucose deprivation, presence of mutant proteins or even increased production of normal secretory proteins can trigger the ER stress response [5].
In contrast, overproduction of the mutant Sec62 protein, even in the presence of the endogenous Sec62-WT protein, reduced cell migration in a manner similar to SEC62 silencing.
The wild-type and Q766H forms of the enzyme restored viability of the yeast double deletion mutant, demonstrating that the human proteins – even the Q766H mutant in the catalytic domain – were catalytically active in yeast cells.
Given simulations from related mutant proteins, MD simulations could even predict the atomic level effects of mutations.
Other mutants produced localized fusion proteins even though the transposon has inserted near the 5' end of a gene, demonstrating that short peptides can contain sufficient information to localize bacterial proteins.
The mutant protein is folded even in the absence of metals, and variants that retain the original activity of thioredoxin can be isolated.
And even if the mutant proteins are present, he says, "they are much more likely to be an effect than a cause" of AD brain damage.
