The Center of Biomedical Research Excellence (COBRE) in Membrane Protein Production and Characterization at the University of Delaware was established in 2000 with generous support under the COBRE program within the National Center for Research Resources (NCRR) of the National Institutes of Health (NIH). Additional support was provided by the Delaware Biotechnology Institute (DBI). In its original form the COBRE supported research covering a broad range of activities in Structural and Functional Genomics, but the present focus on membrane protein production and characterization was adopted following renewal of the program in 2005. The program was renewed again as a Phase III center in 2010; within this structure it is primarily an infrastructure center that provides direct support for shared core facilities and pilot projects, but the participating investigators involved in the center have independent support for their membrane protein research that draws on center resources and contributes to the overall research progress in the center.
Why membrane proteins?
Membrane proteins are critical for cell-cell recognition, inter- and intracellular signaling, transmembrane transport and cell homeostasis, and are of great interest in understanding human disease and as drug targets. It is estimated that membrane proteins represent >30% of the human genome and are the targets of >50% of all therapeutics on the market today. However, only a small fraction of these important proteins have been isolated, the functions of most of them remain unknown, and membrane proteins make up < 1% of solved high-resolution structures in the Protein Data Bank. Reasons for this lag in membrane protein characterization include difficulties in expressing such proteins in significant quantities, in isolating and purifying them in view of their amphipathic character, and in crystallizing them. The COBRE in Membrane Protein Production and Characterization undertakes research to help overcome these difficulties and to elucidate the biological functions of additional membrane proteins.