A team of researchers from Penn State and the University of Texas Southwestern Medical Center has discovered a way to use light to control certain proteins that catalyze biochemical reactions. "This is one of the first examples of someone successfully controlling the activity of a protein using light," said Stephen Benkovic, Penn State Evan Pugh Professor of Chemistry, holder of the Eberly Family Chair in Chemistry, and one of the team's leaders. "The technology one day could be expanded to have multiple uses, including the ability to turn off the activities of some disease-causing proteins in the cell," he said. The team's results will appear in the 17 October issue of the journal Science.
In their experiment, the scientists designed a hybrid protein by inserting a light-sensing protein from an oat plant into an enzyme -- a type of protein that catalyzes biochemical reactions -- from the bacterium E. coli. After engineering the two components together, the researchers found that the enzyme's activity could be manipulated by shining a light on the light-sensing protein, which the scientists refer to as a "domain." "The technology works like a light switch," said Benkovic. "When we shine a light on the light-sensing domain, the enzyme's activity increases, and when we shut the light off, the enzyme's activity decreases."
According to Jeeyeon Lee, a postdoctoral scholar in the Penn State Department of Chemistry and one of the paper's authors, the team had to consider a number of factors when designing the hybrid protein, including the protein's shape, or what is referred to as its conformation. "The conformation of a protein is important in determining its function," she said. "Without the proper conformation, our protein would not have responded to the light."
Another important factor that the team had to consider was the proper location on the enzyme into which the light-sensing protein from the oat plant would be i
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