Sen. Lugar meets with Purdue biofuels researchers, tour labs and Purdue Research Park
U.S. Sen. Richard G. Lugar on Thursday (Oct. 9) met with Purdue University biofuels and alternative energy researchers and toured campus research facilities at Discovery Park and the Purdue Research Park.
The Republican senator heard presentations from biofuel, biotechnology and hydrogen storage researchers at Purdue's Laboratory for Renewable Resource Engineering (LORRE) and Birck Nanotechnology centers in Discovery Park. He also toured facilities at Swift Enterprises Ltd., a Purdue Research Park-based company developing a lead-free, alternative aviation fuel. Lugar met with Purdue President France A. Córdova and Victor L. Lechtenberg, vice provost for engagement, and joined a tour of research laboratories led by Alan Rebar, executive director of Purdue's Discovery Park.
Seed for Success Awards
The Seed for Success Awards were established by the Office of the Provost and the Office of the Vice President of Research to recognize faculty members who have attracted an individual sponsored research grant to Purdue University in excess of $1 million.
“Structure and Function of Flaviviruses” - Michael G. Rossmann, Jue Chen, Richard J. Kuhn
“Development of the www.EcoliCommunity.org” - Barry L. Wanner (PI), Walid G. Aref, Michael R. Gribskov, Daisiuke Kihara
Symposium on Frontiers in Biological Membranes
October 16 - 18, 2008
Dean’s auditorium and gallery, Pfendler Hall
More information
Symposium pdf
Structure Captures Toxin Peptide in Transit across a Membrane Channel Protein
A team of scientists led by Prof. W. A. Cramer, the Henry Koffler Distinguished Professor, has obtained a crystal structure of OmpF (“outer membrane protein F”), a major pore protein in the outer membrane of the E.coli bacterium, alone (see Figure) and in complex with a toxin peptide. OmpF serves as an aqueous conduit through the hydrophobic membrane, thereby allowing the bacteria to take up important nutrients necessary for its survival, and is a model structure for studies on the flow of water and solutes in the narrow channels that resemble nanotubes. The 1.6 Å resolution structure reveals the detailed distribution of water molecules within the trans-membrane channel. An additional structure of OmpF solved by the same team showed the OmpF pore to contain an unfolded protein fragment derived from a specialized “colicin E3” toxin. The structure confirms a previous hypothesis from the Cramer group that colicin toxins parasitize membrane receptors such as OmpF to enter the bacterial cell where they subsequently exert their cytotoxic effect. The toxin-porin structure is the first of its kind and provides a major advance in understanding of the mechanism of protein transfer across biological membranes. These studies were recently (August 6, 2008) published in the EMBO (European Molecular Biological Organization) Journal. Co-workers and co-authors were E. Yamashita (Institute of Protein Research, Osaka Univ., Japan), and M. V. Zhalnina,
Dr. S. D. Zakharov, and Dr. O. Sharma in the Dept. of Biological Sciences.
