After in vitro expression, mutants were tested for functionality.
Subsequently, these mutants were tested in lab-scale vinifications to select low-ethanol yeasts.
For species comparison, a subset of cTnI mutants were tested in isolated adult rabbit cardiac myocytes.
The wild-type TsPOx and its four mutants were tested for their effect on enlarging the loaf volume in breadmaking.
These mutants were tested for their ability to cleave and to catalyze asparagine hydrolysis, in addition to being examined structurally.
All mutants were tested for their ability to form geranylated hydroxybenzoate from geranyl diphosphate, but only the unmodified UbiA-enzyme and to minor extent one mutant showed enzymatic activity.
Wild type and mutants were tested in vitro; they had an activity of at least 45% of the wild type and showed markedly altered enantioselectivity, mutant L287W had even reversed enantiopreference.
All E6 mutants were tested for their ability to degrade p53 using the Western blot assay.
Eight double alanine mutants were tested, in which we primarily focused on charged and hydrophobic residues.
All phage mutants were tested individually for their binding to RD cells (Fig. 3A).
Both conjugation to various UbcHs and total ISGylation patterns of different HuISG15 mutants were tested.
