Written by John Finn 330-263-2145 Email Story | Print Story

May 17, 2004

Recipients of a $320,300 National Science Foundation grant are (clockwise from left): Mark Snider, assistant professor of chemistry, Dean Fraga, associate professor of biology, and Paul Edmiston, assistant professor of chemistry.

WOOSTER, Ohio - A sudden burst of energy. For world-class athletes headed to the Olympic Games in Athens this summer, it could be the difference between Gold and Silver. For smaller, less-heralded organisms, it could be the difference between life and death.

At the heart of it all is an enzyme involved in the muscle function of most, if not all, organisms, which helps maintain a reserve of energy for use when these sudden bursts are required, and three scientists at The College of Wooster are working collaboratively to learn more about it.

Mark Snider, assistant professor of chemistry and principle investigator (PI) for the grant, Paul Edmiston, assistant professor of chemistry and co-PI, and Dean Fraga, associate professor of biology and co-PI , have been awarded a three-year, $320,300 grant from the National Science Foundation to study the nature of this enzyme and how it functions.

The project was originally started by Charles Borders, professor of chemistry emeritus at Wooster. "Through his enthusiasm, the three of us became interested in and excited about the project," says Fraga. "Following his retirement, we decided to continue and expand on his work because it provided a perfect context for engaging in collaborative research and a wonderful forum for teaching students basic scientific skills. It is an affirmation of a growing partnership between the departments of chemistry and biology."

The grant supports three interlinked projects designed to get at several fundamental questions about this important enzyme, which uses the protein creatine kinase to provide short, sudden bursts of energy often required in muscles.

People may remember that several years ago creatine was a rage among athletes, who would "load up" before an event in the hopes of unleashing that sudden burst of energy at just the right moment. Snider points out that the process is much more complicated. "Excessive amounts of creatine have little value and cell's cannot store much of it," he says. "What we are trying to determine is what makes this happen. How does the protein work fundamentally?"

The first question that Fraga, Edmiston, and Snider will ponder is why the enzyme is built the way it is. "We're looking at how a particular structure dictates specific biochemical functions, much as one might ask how a building's structure dictates its function," explains Fraga. "For example, a restaurant is built much differently than a motel because the functions of each is different."

The second question to be addressed by the three scientists is how this enzyme evolved into the various forms and functions that are present today. "We see many different forms of phosphagen kinase in various species," says Fraga. "We would like to learn why these differences exist."

The third question is how the biochemical differences in this enzyme family result in different physiological functions across organisms. In other words, can the small differences in biochemical structure and function be measured, and do they result in differences in observed physiological functions of organisms? "Intriguingly, we have also identified five unique forms of the enzyme in a single organism," explains Snider. "One of things we hope to discern is whether the five forms perform different functions, or if their functions are redundant. At first glance, there appear to be some exciting new mechanisms to be explored."

These questions will be addressed by using a combined biochemical and molecular biology approach that will involve up to 45 Wooster students over the next three years. The grant will support the research and be used to purchase equipment and supplies necessary to conduct these experiments, including the removal of the protein from a cell. "One way to determine the function of something is to take it out and see what happens," says Fraga. "We will be looking at performance in micro-organisms with and without this protein."

While the research is narrowly focused, Edmiston says that the three researchers have the big picture in mind. "Our interest is in how and why proteins evolved the way they did," he says. "Investigating this family of enzymes is like looking at a huge picture with a very small flashlight."

Wooster's NSF grant was one of seven given the highest possible rating among 89 proposals, including a number submitted by large research universities. Overall, only 15-20 percent of all submitted proposals were funded by the Metabolic Biochemistry program. "We are grateful for the opportunity to carry on the research," says Fraga. "Forming this core research group gives us an opportunity to work across disciplines in the areas of biochemistry and molecular biology to solve a problem of mutual interest."