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Our Western blot results indicate that the mutant proteins do not in general suffer from low stability, with the possible exception of EndoAΔLQPNP.

These two mutant proteins do not bind F-actin either (Figure 6F, supplementary Figure S5) due to defects in the highly conserved helix-4, which is essential to the binding of F-actin [28], [36], [38], [40].

We also have not observed any dominant phenotypes associated with any of these alleles, further suggesting that the mutant proteins do not interfere with other molecular processes, for example by forming inactive complexes.

Therefore, one possible distinguishing feature of this mutation is that the mutant NC1 domains do not fold or function properly and thus, the mutant proteins do not participate in heterotrimer formation.

Expression of disease-mutant strumpellin on a wild-type background did not cause a phenotype, suggesting that the mutant proteins do not act by a dominant negative effect [8].

Similar(55)

Taken together, these results indicate that the distribution of our mutant proteins does not correlate with their metabolic stability.

Production of both mutant proteins did not result in increasing peroxisome numbers.

Consistent with these results, AtLYK5S206P mutant proteins did not bind to chitin beads, while AtLYK5Y128G mutant proteins showed a strong reduction in chitin binding using this same assay.

Comparison of relative CTPsyn abundances indicates that most of the mutant proteins did not result in an apparent change in protein abundance.

At a concentration of 150 nM enzyme/300nM substrate, we observed that the dimeric IKK2EE(11–669) could turn over product, whereas various IKK2mono mutant proteins did not display activity.

Protein analysis confirmed that while total mutant protein did not differ from wild type, membrane expression of the mutant channel was substantially reduced.

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