Toward a Biology Worthy of Life > The Unbearable Wholeness of Beings > Brief excerpt
A project by Stephen L. Talbott

The virtue of “disordered proteins” (1)

Nor is it the case that proteins must choose in a neatly digital fashion between discrete conformations. In contrast to the old “rigid-body” view, researchers now refer to “fluid-like” and “surface-molten” protein structures (Grant et al. 2010; Zhou et al. 1999). Even more radical has been the discovery that many proteins never do fold into a particular shape, but rather remain unstructured or “disordered.” In mammals, about 75% of signaling proteins and half of all proteins are thought to contain long, disordered regions, while about 25% of all proteins are predicted to be “fully disordered” (Uversky 2010). Many of these intrinsically unstructured proteins are involved in regulatory processes, and are often at the center of large protein interaction networks (Gsponer and Babu 2009).

Fluid, “living” molecules do not lend themselves to the analogy with mechanisms, which may explain why the mistaken idea of precisely articulated, folded parts was so persistent, and why the recognition of unstructured proteins has been so late coming.

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