Research

Institute for CyberScience faculty member wins $1.9 million NIH award

"By creating physics- and chemistry-based models, we can explore the origins and consequences of translation rate changes on protein behavior," said O'Brien. Credit: Nate Follmer / Penn State. Creative Commons

UNIVERSITY PARK, Pa. — Edward O'Brien, assistant professor of chemistry, Penn State and an associate with the University's Institute for CyberScience (ICS), has received a grant for $1.9 million over 5 years from the National Institutes of Health. The award will support fundamental research on how proteins form.

O'Brien's study, "Modeling the influence of translation-elongation kinetics on protein structure and function," will investigate how the speed at which a protein is assembled — the translation rate — affects the protein's ability to fold and function properly. The question is groundbreaking because until recently most scientists did not believe that translation rate impacted protein function at all. Researchers are still unsure exactly why a protein's translation rate affects its behavior, but O'Brien aims to find out.

His team is developing computer simulations to model the mechanics of protein translation. The simulations will be computationally intensive, so the team plans to use ICS's Advanced CyberInfrastructure, Penn State's high-performance research cloud. Using many powerful computer cores at once, the model will provide results quickly.

"By creating physics- and chemistry-based models, we can explore the origins and consequences of translation rate changes on protein behavior," said O'Brien. "This project will increase our understanding of protein synthesis in ways that could help us combat debilitating diseases."

Just as musical notes arranged in a certain order form a song, chains of amino acids that are arranged in specific sequences form the proteins from which our muscles and tissues are made. For half a century, scientists believed that the order of the amino acids was the only factor governing how a protein functioned. But new evidence demonstrates that mutations that change a protein's translation rate can cause the protein to malfunction, even if the order of the amino acids is correct. Learning how translation rate affects these malfunctions could be key to understanding several diseases, including cystic fibrosis and some varieties of lung, cervical and vulvar cancer.

"Ed O'Brien's research has amazing potential to advance the field of proteomics in ways that will impact human health, and he fully deserves this grant," said ICS Director Jenni Evans. "His project embodies the kind of transformational computational work that ICS is proud to support."

Last Updated August 10, 2017

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