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By contrast, there was an increase in fluorescence when an equimolar mixture of both mutants was tested, indicating that CaM bridges the two proteins41 (see supplemental Fig. 6D).
To determine its function, an analysis of deduced amino acid sequence of the CnCdk1 was performed and its ability to rescue Saccharomyces cerevisiae cdc28-temperature sensitive mutants was tested.
Lack of motility of flgK mutants was tested on motility agar.
The expression of a subset of these promoters was tested in planta using recombinase-based in vivo expression technology (RIVET) and fitness of the corresponding mutants was tested.
Then, an equal amount of F protein from the different mutants was tested for reactivity with non-saturating amounts of VHHs, 0.2 µg/ml in ELISA.
Activity of the mutants was tested with the assay described below.
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After in vitro expression, mutants were tested for functionality.
For species comparison, a subset of cTnI mutants were tested in isolated adult rabbit cardiac myocytes.
Mutants were tested for maintenance of mitochondrial DNA, inhibition of telomerase at telomeres and double strand breaks, and promotion of Okazaki fragment maturation.
These mutants were tested for their ability to cleave and to catalyze asparagine hydrolysis, in addition to being examined structurally.
Subsequently, these mutants were tested in lab-scale vinifications to select low-ethanol yeasts.
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