“A picture is worth 1,000 words, and very often, getting a first three-dimensional view of a component of the cell gives you valuable insight - often surprising and unexpected - that you could not anticipate. “The last 50 years of structural biology has been about trying to get detailed pictures of all the parts of the cell to understand them thoroughly,” Yeates said. Why is it so important to see a protein in such detail? The development of cryo-electron microscopy earned Jacques Dubochet, Joachim Frank and Richard Henderson the 2017 Nobel Prize in Chemistry. “The small protein we attached can itself be made to bind to other proteins, which can then be studied by cryo-electron microscopy,” said Yeates, whose research team is currently working on doing this. Their new method, which Yeates calls “scaffolding,” can be modified easily to bind to many different proteins as a “universal protein scaffold.” But when the researchers attached the copies to the protein cage, they succeeded in seeing the DARPin with cryo-electron microscopy.Ī challenge the researchers overcame was getting the copies of the protein to attach in a rigid manner. The small protein, called a DARPin, is too small to analyze using cryo-electron microscopy alone. In the new research, his team used “protein engineering” to attach 12 copies of a small protein to a cube-shaped molecular cage, which was designed by a former graduate student of Yeates’. Yeates’ research team published the first research, in 2001, in the scientific field of designing molecular cages built from protein molecules. Image depicts molecular “scaffolding.” The molecular cage is in yellow and blue the DARPin protein is in red.
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