The funding will allow the Haverford chemistry professor and his lab to use new methods to study the structural changes that occur when proteins bind to other proteins. The lab's research could shed light on several common diseases associated with disordered proteins.
Assistant Professor of Chemistry Casey Londergan has received an AREA (Academic Research Enhancement Award) from the National Institute of General Medical Sciences—the basic research arm of the National Institutes of Health (NIH)—for a project focusing on the structure and binding of proteins. The award provides Londergan with $202,355 for two years of work, and is funded in part by the U.S. economic stimulus package, because of its contributions to NIH.
The grant allows Londergan to use new experimental methodology—which he developed with students in his Haverford lab during the past three years—to study the structural changes in proteins when they bind to other proteins.“Our methodology gives us a new way to view a small, chosen piece of a protein, through its absorption of infrared light,” he says. “If there is a change in that selected part of a protein, then we can see that.” Londergan and his collaborators hope to build an experimental“map” of how a protein's structure changes when it binds to another protein.
“Understanding protein-protein interactions is very important given how crowded cells are,” says Londergan.“But proteins that bind to multiple partners usually have very dynamic shapes, and they are difficult to characterize using more traditional biochemical techniques. We hope that our novel approach is able to help.”
Londergan and colleagues will examine two specific proteins as test cases for this new technique: a piece of the measles virus and calmodulin, a calcium-binding protein used by many organisms in different kinds of cells to convey regulatory signals. He is working with a group in Marseilles, France, to examine the interaction between two viral proteins essential to the assembly of the measles virus, and will map the structure of some calmodulin complexes with scientists in Lund, Sweden.“The grant provides funds for Haverford students to travel to the laboratories of our international collaborators to prepare protein samples for experiments performed here at Haverford,” says Londergan.
Londergan's research has public health implications: His new approach to studying proteins may make it possible to understand the molecular basis of diseases associated with disordered proteins.“Proteins with disordered structures often have malleable shapes, and thus are able to bind to many different physiological partners,” he says.“This means that their dysfunction is often associated with systematic diseases like cancer or neurodegenerative diseases like Alzheimer's and Parkinson's.”
Londergan is honored to receive the award.“This grant gives my group a much greater range of options in our research,” he says.
