Applications
Applications
- Recently
our group has engineered fusion proteins which combine a repetitive B-sheet
domain and a link to one monomer of the phosphotriesterase enzyme.
- This work began before the crystal structure was determined,
and biochemical studies did not indicate the enzyme formed a dimer in solution,
and is not reflected by this image.
- The B-sheet domain can be modified so it adheres to a
substrate, such as glass.
- Rate studies have shown that the enzyme retains most
of its activity even while contrained to a substrate surface, but any perturbations
in its conformation, while expected, have not been characterized.
- This fusion protein has been demonstrated as a means
of detecting organophosphates such as paraoxon and sarin.
- The hydrolysis products of the reaction (see mechanism)
are very strongly colored, and produce a yellow color as shown in the two
liquid chromatography columns to the right.
- The right column has only glass beads, while the left
column has glass beads bound to the fusion protein.
This work was performed by Dong Wu in D.A. Tirrell's group, in press.