To validate the method, randomly generated xylanase mutants were analyzed.
Secondary and tertiary structure of mutants were analyzed by CD and fluorescence spectroscopy.
The reaction kinetics of all the mutants were modeled, and the pH and thermal stabilities of all the mutants were analyzed.
The hydrodynamic and self-associative properties of a series of PaDDAH interface mutants were analyzed by concentration-dependent analytical size-exclusion chromatography and sedimentation equilibrium analytical ultracentrifugation.
Under a programmed electric field strength and a sieving gel matrix of 0.7% poly ethylene oxide) (Mr=8,000,000), T-DNA-inserted rice mutants, two standard wild-type rice lines, and six rice knockout mutants were analyzed within 4 min using three parallel channels on the microchip.
The properties of the deletion mutants were analyzed.
All mutants were analyzed in CHO cells using the whole-cell patch-clamp technique.
Resulting mutants were analyzed by PCR to ensure the loss of the hlyA gene.
To further characterize the behavior of the 21- and 22-nt miR168 species, mir168a and mir168b mutants were analyzed.
Three mutants were analyzed, prtE, outC and hrcC impaired in type I, II and III secretion systems respectively (Fig. 1A).
Purified L1ICD mutants were analyzed by Western blot analysis with an anti-L1 antibody, which recognizes the unmutated form of L1ICD.
