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Radiolytic footprinting of membrane-bound rhodopsin

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This approach demonstrates the structural activation of bound waters as a function of receptor signaling status. X-rays ionize water molecules inside and outside the membrane protein to radicals (see o OH, glowing spheres) that react with adjacent amino a

Credit or Source: For more details, see Angel, T. E., et al. 2009. "Structural Waters Define a Functional Channel Mediating Activation of the GPCR, Rhodopsin," Proceedings of the National Academy of Sciences of the United States of America 106(34), 14367-72.

Citation(s):

U.S. DOE 2012. Applications of New DOE National User Facilities in Biology Workshop Report, DOE/SC-0147, U.S. Department of Energy Office of Science. (p. 75) (PDF)

Brookhaven National Laboratory