IDPs: Dancing Proteins and the Search for New Therapies

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Our Internal Misfits

Proteins are very important for life. They cut, build, defend, carry, and control things. For years, we’ve been told that they can only do these jobs if they fit into a certain, stable three-dimensional shape. That shape, which is made up of a string of amino acids, is like a tool that has been finely tuned for its job. A hammer and a screwdriver don’t work the same way. Similarly, the structure of a protein should tell you what it does. But there’s a twist in this story.

In the past two decades, scientists learned that most crucial proteins do not fold at all. They don’t fit into any set shape. Rather, they behave like cooked spaghetti; floppy, random, and constantly changing shape. They are Intrinsically Disordered Proteins, or IDPs. According to the study, “The molecular basis for cellular function of intrinsically disordered protein regions”, published in the Molecular Cell Biology journal, these IDPs have turned out to be key players in the body, especially in challenging roles like gene expression, stress response, and immune defence. In fact, some of the most dangerous disease-linked proteins, like those involved in Alzheimer’s, cancer, and viral infections, are disordered…read more NOPR