Category:Team Kary Mullis

Figure 1 shows that inducing the synthesis of KinA during growth triggers efficient sporulation.

Figure 3

Figure 4 shows KinA synthesis triggers sporulation early in the exponential phase of growth.

Fig. 5 indicates that SirA reduces the amount of wild-type but not mutant DnaA bound at the origin of replication. Therefore this results indicate that interaction of SirA contacts DnaA at a patch of 3 residues located on the surface of domain I of the replication initiator protein and inhibits the ability of DNA to bind to the origin of replication.

NADPH-binding domain must rotate 60° relative to the FAD-binding domain in order for hydride (movement of electrons and protons) transfer to take place as seen as figure 2d.

Table 4

Figure 1

Figure 4. Immunoblot

Table 4. Table 5

Table 4. Table 5

Table 4. Table 5

"The refined crystallographic structure of the "closed" conformation of chicken mitochondrial aspartate aminotransferase has been used as a template for the construction of models of the two Escherichia coli aminotransferases encoded by the tyrB and aspC genes"

Figure 4 indicates the purified Gid protein catalyzes the site-specific formation of m5U-54 in [32P]-labeled yeast tRNAAsp transcript.

Figure 2A and B indicate that the wild type cell extract was able to catalyze formation of m^5U-54 in vitro, however the mutant strain lacking the functional Gid protein was unable to catalyze such a methylation reaction. Thus this indicates that the gid gene product is involved in product of m^5Y-54 in tRNA.

Figure 6.

Figure 4

Figure 1 indicates a decrease in optical rotation as a results of a structural change observed in the alpha position of the L-glutamate substrate. This results are observed during the incubation with glutamate racemase in deuterium oxide.

Figure 2