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Metamorphic proteins are able to drastically switch between multiple shapes in human, animal and bacterial cells, enabling them to adapt to changing environments and carry out diverse functions. But L ittle is known about how this “shapeshifting” happens.
To help solve this mystery, a new perspective paper published Monday in the journal Proceedings of the National Academy of Sciences (PNAS) offers a “bold theory,” said co-author John Orban, a professor in the University of Maryland’s Department of Chemistry and Biochemistry and Institute for Bioscience and Biotechnology Research (IBBR).
Orban and co-author Andy LiWang, a professor of chemistry and biochemistry at the University of California, Merced, suggest that all metamorphic proteins have an “underlying temperature dependence.” If confirmed, this would mean that temperature—cold temperature in particular—plays a fundamental role in setting off shapeshifting in metamorphic proteins.
Ultimately, a better understanding of metamorphic proteins could advance biomedical research and the development of lifesaving drugs.
“It may be possible to design proteins that are switchable and have more than one function,” Orban said. “They could potentially be stealth proteins that go into a cell and pretend to be one state, but under certain environmental conditions switch to a state that could kill the cell—which, if it's a cancer cell, might be a good thing.”
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