This is the best summary I could come up with:

The complex three-dimensional shapes that proteins adopt create folds and pockets that can accomplish the remarkably improbable: driving chemical reactions that would otherwise never happen or binding to a single chemical inside the complex environment of a cell.

People haven’t been sure whether these proteins temporarily adopted a specific structure to work or the disorder was critical for function.

Now, a new paper describes a case where two intrinsically disordered proteins induce specific structures in each other when they interact.

Most studies of protein structures identify the positions of amino acids with a fairly high degree of certainty.

Eventually, people came around to the idea that this seemingly disordered state was not an experimental artifact but, rather, represented the protein’s actual behavior—and, in some cases, was essential to their function.

The regions of both NuMA and protein 4.1G that mediate this interaction have been identified, and they’re both intrinsically disordered.

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