Thirty percent of all proteins are not soluble but are embedded in membranes, she explained. "These membrane proteins, major players in the function of all living cells, are the targets for more than 50 percent of all drugs, yet, scientists have a lack of information on their structure and function. While more than 60,000 structures of soluble proteins have been determined to date only 256 membrane proteins structures are known and only four of them are human membrane proteins," said Fromme, who directs ASU's new Center for Membrane Proteins in Infectious Diseases, one of nine centers set up by the National Institutes of Health to decipher the structures of membrane proteins.
"This milestone research reported in Nature opens a new avenue for solving protein structures and will have a huge impact in a lot of areas, including development of clean energy and the medical field," she said. "The determination of the protein structure will lead to the development of new drugs against cancer and infectious diseases, by manufacturing drugs that fit into the catalytic center of the proteins like a perfect key in a lock."
For the nanocrystallography experiments, which took place in December 2009 at SLAC in California, Fromme's lab at ASU supplied nanocrystals of photosystem I, a large membrane protein complex consisting of more than 100,000 atoms that acts as a biosolar energy converter in the process of oxygenic photosynthesis.
Protein crystals contain a lot of liquid and are "extremely weak, like a piece of butter in the sun," Fromme explained. "When you just touch them, they're destroyed." It had taken her group 13 y
|Contact: Carol Hughes|
Arizona State University