Disorder enhances binding cooperativity

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Science  21 Nov 2014:
Vol. 346, Issue 6212, pp. 961
DOI: 10.1126/science.346.6212.961-b

Some natural proteins, such as hemoglobin, bind their ligands in a cooperative manner, whereby the binding of the first ligand alters the structure of the protein, favoring binding of subsequent ligands. Taking inspiration from this mechanism, Simon et al. created unstructured receptors from DNA. Upon binding their ligand, the disordered receptors become structured, forming sites for further ligands to bind. Because ligands bind more favorably to these sites than to the unstructured receptor, the binding of subsequent ligands is enhanced. Relatively small changes in ligand concentration can therefore lead to an all-or-none binding response, a feature that could prove useful for artificial biotechnologies.

Proc. Natl. Acad. Sci. U.S.A. 10.1073/pnas.1410796111 (2014).

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