Researchers discover a way to strengthen proteins

Dec 10, 2009

Proteins, which perform such vital roles in our bodies as building and maintaining tissues and regulating cellular processes, are a finicky lot. In order to work properly, they must be folded just so, yet many proteins readily collapse into useless tangles when exposed to temperatures just a few degrees above normal body temperature.

This precarious stability leaves proteins and the living beings that depend upon them on the edge of a precipice, where a single destabilizing change in a key protein can lead to disease or death. It also greatly complicates the manufacture and use of proteins in research and medicine.

Finding a way to stabilize proteins could help prevent such dire consequences, reduce the very high cost of protein drugs and perhaps also help scientists understand why proteins are often so unstable in the first place. In a paper published in the Dec. 11 issue of the journal Molecular Cell, researchers at the University of Michigan and the University of Leeds describe a new strategy for stabilizing specific proteins by directly linking their stability to the of bacteria.

"The method we developed should provide an easy way to strengthen many proteins and by doing so increase their practical utility," said James Bardwell, a Howard Hughes Medical Institute investigator and professor of molecular, cellular and at U-M.

In the new approach, the researchers found that when a protein is inserted into the middle of an antibiotic resistance marker, bacterial antibiotic resistance becomes dependent upon how stable the inserted protein is. This enabled the scientists to easily select for stabilizing mutations in proteins by using a simple life-or-death test for on antibiotics. The mutations the scientists identified rendered proteins more resistant to unfolding.

"This method also has allowed us to catch a glimpse of why proteins may need to be just barely stable," said Linda Foit, the graduate student at U-M who initiated the work. "The mutations that we found to enhance the stability of our model protein are mostly in key areas related to the protein's function, suggesting that this protein may need to be flexible and therefore marginally stable in order to work. It may be that, over the course of evolution, natural selection acts to optimize, rather than maximize stability."

Source: University of Michigan (news : web)

Explore further: Bulletproof nuclei? Stem cells exhibit unusual absorption property

add to favorites email to friend print save as pdf

Related Stories

Building a better protein

Feb 23, 2009

Proteins are widely viewed as a promising alternative to synthetic chemicals in everything from medications to hand lotion. The naturally occurring molecules have been shown to be more efficient and effective than many of ...

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 ...

Engineers squeeze secrets from proteins

Mar 21, 2006

Proteins, one of the basic components of living things, are among the most studied molecules in biochemistry. Understanding how proteins form or "fold" from sequenced strings of amino acids has long been one of the grand ...

Yale scientists map cell signaling network

Nov 30, 2005

Yale University scientists have mapped, for the first time, the proteins and kinase signaling network that control how cells of higher organisms operate.

Recommended for you

Researchers successfully clone adult human stem cells

Apr 18, 2014

(Phys.org) —An international team of researchers, led by Robert Lanza, of Advanced Cell Technology, has announced that they have performed the first successful cloning of adult human skin cells into stem ...

Researchers develop new model of cellular movement

Apr 18, 2014

(Phys.org) —Cell movement plays an important role in a host of biological functions from embryonic development to repairing wounded tissue. It also enables cancer cells to break free from their sites of ...

User comments : 0

More news stories

Biologists help solve fungi mysteries

(Phys.org) —A new genetic analysis revealing the previously unknown biodiversity and distribution of thousands of fungi in North America might also reveal a previously underappreciated contributor to climate ...

Making graphene in your kitchen

Graphene has been touted as a wonder material—the world's thinnest substance, but super-strong. Now scientists say it is so easy to make you could produce some in your kitchen.