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ORNL fundamental discovery casts enzymes in new light
Date:11/9/2011

OAK RIDGE, Tenn. -- A tree outside Oak Ridge National Laboratory researcher Pratul Agarwal's office window provided the inspiration for a discovery that may ultimately lead to drugs with fewer side effects, less expensive biofuels and more.

Just as a breeze causes leaves, branches and ultimately the tree to move, enzymes moving at the molecular level perform hundreds of chemical processes that have a ripple effect necessary for life. Previously, protein complexes were viewed as static entities with biological function understood in terms of direct interactions, but that isn't the case. This finding, published today in PLoS Biology, may have enormous implications.

"Our discovery is allowing us to perhaps find the knobs that we can use to improve the catalytic rate of enzymes and perform a host of functions more efficiently," said Agarwal, a member of the Department of Energy laboratory's Computer Science and Mathematics Division.

Making this discovery possible was ORNL's supercomputer, Jaguar, which allowed Agarwal and co-author Arvind Ramanathan to investigate a large number of enzymes at the atomistic scale.

The researchers found that enzymes have similar features that are entirely preserved from the smallest living organism bacteria -- to complex life forms, including humans.

"If something is important for function, then it will be present in the protein performing the same function across different species," Agarwal said. "For example, regardless of which company makes a car, they all have wheels and brakes."

Similarly, scientists have known for decades that certain structural features of the enzyme are also preserved because of their important function. Agarwal and Ramanathan believe the same is true for enzyme flexibility.

"The importance of the structure of enzymes has been known for more than 100 years, but only recently have we started to understand that the internal motions may be
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Contact: Ron Walli
wallira@ornl.gov
865-576-0226
DOE/Oak Ridge National Laboratory
Source:Eurekalert

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