The researchers strategy was to split the amino acid tag for the dye into two pieces, locating each piece of the tag far apart in the chain of a protein they genetically engineered and expressed in the cells. Then they monitored cells exposed to the dye. Where the protein folded correctly, the two parts of the tag came together and the fluorescent compound bound and lit up. There was no signal unless the protein folded normally.
This method of detection can provide important insights into how proteins choose their partners within the cell choices that may be very different from those made in a test tube, said Schepartz. She emphasizes that this technology does not monitor the process of protein folding but, rather sees the protein conformations that exist at a given time.
In theory, our technique could be used to target and selectively inactivate specific protein complexes in the cell, as therapy, or to visualize conformations at very high resolution for diagnostic purposes, said Schepartz. She speculates that the technology could be applied to detection strategies that identify protein misfolding in neurodegenerative diseases like Alzheimers or Parkinsons.
|Contact: Janet Rettig Emanuel|