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The University of Southampton

Research project: Levitt: Solid-State NMR of Rhodopsin

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When light enters the retina at the back of our eyes it is absorbed by a protein called rhodopsin. Rhodopsin absorbs the light energy, initiating a sequence of biochemical events that culminate in a signal being transmitted down the optic nerve to the brain.

Hundreds of millions of years of evolution have led to rhodopsin molecules that are highly sensitive to light but without being too sensitive, and that utilize the light energy extremely effectively, minimizing undesirable side reactions. A great deal can be learnt by studying how this protein utilizes the light energy. We are doing this by studying the protein using solid-state NMR, in the presence of light illumination at temperatures low enough to allow us to stop the light-induced chemical reactions in their tracks.

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Figure: Molecular structure of rhodopsin, showing the light-sensitive retinal chromophore (black).



M. Carravetta, X. Zhao, O. G. Johannessen, W. C. Lai, M. A. Verhoeven, P. H. M. Bovee-Geurts, P. J. E. Verdegem, S. Kiihne, H. Luthman, H. J. M. de Groot, W. J. de Grip, J. Lugtenburg and M. H. Levitt, "Protein-induced bonding perturbation of the rhodopsin chromophore detected by double-quantum solid-state NMR," J. Am. Chem. Soc. 126, 3948 - 3953 (2004).

W. C. Lai, N. McLean, A. Gansmüller, M. A. Verhoeven, G. C. Antonioli, M. Carravetta, L. Duma, P. H. M. Bovee-Geurts, O. G. Johannessen, H. J. M. de Groot, J. Lugtenburg, L. Emsley, S. P. Brown, R. C. D. Brown, W. J. DeGrip, and M. H. Levitt, "Accurate Measurements of 13C-13C J-couplings in the Rhodopsin Chromophore by Double-Quantum Solid-State NMR", J. Am. Chem. Soc., 128, 3878-3879 (2006).

Related research groups

Magnetic Resonance
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