PerspectiveStructural Biology

Snapshots of a protein quake

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Science  23 Oct 2015:
Vol. 350, Issue 6259, pp. 381
DOI: 10.1126/science.aad3371

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“Everything that living things do can be understood in terms of the jigglings and wigglings of atoms,” Richard Feynman famously surmised (1). This question has captured the imagination of biologists since the first protein structure, that of myoglobin, an oxygen (O2) carrier in muscles, was solved by x-ray crystallography (2). Myoglobin binds carbon monoxide (CO) two orders of magnitude more strongly than O2. Bound CO can be dislodged from the active-site heme by light, and the subsequent structural response of the protein has been the focus of intense study by spectroscopic (3), x-ray scattering (4), and x-ray diffraction (XRD) (5, 6) methods, yet complex structural questions remain (7). On page 445 of this issue, Barends et al. (8) provide three-dimensional snapshots of structural changes in myoglobin—low-amplitude collective motions that rapidly spread throughout the protein—that occur during the first few picoseconds (9) after the CO photodissociation.