Scientists devise method to study membrane proteins

Apr 14, 2004

Scientists at the University of Virginia Health System have come up with a protocol to extract proteins from membranes by using chemicals that allow them to be reversibly folded and refolded. The proteins can then be studied using crystallography or nuclear magnetic resonance imaging. Their work is detailed in the March 23 issue of the “Proceedings of the National Academy of Sciences” (PNAS) and also on the cover of the journal. The paper can be found on the web at: http://www.pnas.org/cgi/content/full/101/12/4065.

“The majority of drugs on the market today are effective because they work on membrane proteins, but our basic knowledge about these proteins lags far behind that of water-soluble proteins,” said Lukas Tamm, professor of molecular physiology and biological physics at U.Va. “We need to develop systems to get enough of these membrane proteins expressed in a cell culture so we can measure their thermodynamic, or energetic, stability,” Tamm said. “This is of practical interest in designing proteins for therapeutic applications because the proteins need to be kept around for a long time. This protocol developed at U.Va. shows for the first time that these proteins can be taken out of their membrane environment and put back in without losing function,” Tamm said. “We also found that the thermodynamic stability, or energy difference, between the folded and unfolded form of membrane proteins depends on the strength of the membrane “rubber band” that the proteins sit in. This energy difference can be predicted, one key variable in the drug discovery process.”

In a commentary on the findings, also in the March 23 issue of PNAS, James Bowie, a professor with the Molecular Biology Institute at the University of California, Los Angeles, wrote that “the new work opens another door to a more quantitative description of the energetics protein-protein and protein-lipid interactions in the (membrane) bilayer… We are finally beginning to obtain quantitative information about membrane protein structure.”

Working with U.Va. colleague Heedeok Hong, Tamm used an aqueous (water) system and a compound called urea, that unravels proteins, to carry out folding studies on a membrane protein of the Escherichia coli bacterium called OmpA. Tamm and Hong demonstrated that the folding of OmpA into the lipid bilayers of a membrane is a reversible, two-state process. They also demonstrated that elastic forces in bilayers, such as curvature stress, can affect the folding of membrane proteins.


Explore further: Generating broadband terahertz radiation from a microplasma in air

Related Stories

DOJ, FBI acknowledge flawed testimony from unit

34 minutes ago

The Justice Department and FBI have formally acknowledged that nearly every examiner in the FBI Laboratory's microscopic hair comparison unit gave flawed testimony in almost all trials in which they offered evidence against ...

Dawn glimpses Ceres' north pole

41 minutes ago

After spending more than a month in orbit on the dark side of dwarf planet Ceres, NASA's Dawn spacecraft has captured several views of the sunlit north pole of this intriguing world. These images were taken ...

Mountain of electrical waste reaches new peak

52 minutes ago

A record amount of electrical and electronic waste hit the rubbish tips in 2014, with the biggest per-capita tallies in countries that pride themselves on environmental consciousness, a report said Sunday.

Recommended for you

Researchers build real-time tunable plasmon laser

Apr 24, 2015

(Phys.org)—A combined team of researchers from Northwestern and Duke Universities has succeeded in building a plasmon laser that is tunable in real-time. In their paper published in the journal Nature Co ...

Heat makes electrons spin in magnetic superconductors

Apr 24, 2015

Physicists have shown how heat can be exploited for controlling magnetic properties of matter. The finding helps in the development of more efficient mass memories. The result was published yesterday in Physical Review Le ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.