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First major study of mammalian 'disorderly' proteins

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The St. Jude team developed a technique that uses heat to isolate IUPs in large, purified quantities from extracts of a standard type of cultured mouse cells called NIH3T3 fibroblasts. The IUPs were resistant to the heat, unlike more structured proteins, which fell apart. Based on these studies, the investigators were able to classify all proteins into one of three categories: IUPs; intrinsically folded proteins (IFPs, i.e., fully folded into specific shapes); or mixed ordered or disordered proteins (MPs), which have both structured and unstructured parts.

"This work further illustrates that the disorderliness of IUPs isn't just a curiosity," said Charles Galea, Ph.D., a postdoctoral fellow in Kriwacki's lab. "This characteristic is a fundamental part of how these proteins work. So determining their exact nature, including the parts that are disordered, is an important part of understanding how they work. This is especially important in the case of IUPs linked to cancer and other diseases." The paper's first author, Galea, did much of the work on this project.


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Source:St. Jude Children's Research Hospital


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