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New scientific highlights- by MUST PIs Fabrizio Carbone and Ursula Keller (with Sasha Landsman and Cornelia Hofmann)
Proof of concept ERC Grant for Rachel Grange Automated super-resolution polarimetric nonlinear microscope (PolarNon)
Majed Chergui wins RSC Liversidge Award from the Royal Society of Chemistry
New scientific highlights- by MUST PIs Peter Hamm, Majed Chergui, Urs Staub, Steve Johnson, Jörg Standfuss and Gebhard Schertler
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Biological light sensor filmed in action

June 14, 2018

Film shows one of the fastest processes in biology

(Source: PSI News) - Follow the link to see the molecular movies

The molecule retinal is a form of vitamin A and is of central importance to humans, animals, certain algae, and many bacteria. In the retina of the human eye, retinal triggers the process of vision when it changes its shape under the influence of light. In a similar form, certain bacteria also use this reaction to pump protons or ions through the cell membrane. Light energy can be stored in this way, as in the reservoir of an alpine hydropower plant, so that it is available on demand as biological fuel. To ensure efficient utilisation of light, the retinal molecule is embedded in proteins that play a critical role in regulating the process. The protein-regulated reaction of retinal is one of the fastest biological processes and occurs within 500 femtoseconds (a femtosecond is one-millionth of one-billionth of a second). That is roughly a trillion times faster than the blink of an eye, says Jörg Standfuss, who heads the group for time-resolved crystallography in the Division of Biology and Chemistry at PSI. What happens in the process on the atomic level has now been captured for the first time by PSI researchers, in 20 snapshots that they have assembled into a molecular movie. No one has previously measured a retinal protein at such high speed and with such precision. It's a world record, says Jörg Standfuss, who led the study.
The researchers studied the protein bacteriorhodopsin, which is found in simple microbes. When the retinal molecule embedded in the bacteriorhodopsin traps a light particle, it changes its original elongated shape into a curving form, like when a cat arches its back, explains the PSI researcher. Such changes can also be observed when retinal is examined in a solution without protein. There, though, different reactions, which are also less productive, take place. Proteins are like factories in which chemical reactions run especially efficiently, Jörg Standfuss explains. We wanted to look at how this interplay between the protein and the molecule functions.

A surprising observation
The researchers discovered that water molecules in the vicinity of the retinal play a critical role. They were able to observe how the water molecules moved aside and made room for the retinal molecule to do its cat-arching-its-back move – in the technical jargon, a trans-cis isomerisation. This detail, which no one had seen before, surprised Jörg Standfuss, as he explains with the help of the cat analogy: You expect that a cat might arch its back to scare another one away. But here the second cat runs away even before the first has arched its back. Computer simulations confirm the measurements, which could be explained by ultrafast quantum processes.
Besides the retinal reaction, the researchers were also able to detect protein quakes that had been predicted by theory. The arching of the cat's back does not require the entire energy of the light that falls on the protein. Excess energy is released, evidently, not in the form of heat but rather in vibrations of the protein.



See also: SLAC,

Reference: Nogly, P., T. Weinert, D. James, S. Carbajo, D. Ozerov, A. Furrer, D. Gashi, V. Borin, P. Skopintsev, K. Jaeger, K. Nass, P. Båth, R. Bosman, J. Koglin, M. Seaberg, T. Lane, D. Kekilli, S. Brünle, T. Tanaka, W. Wu, C. Milne, T. White, A. Barty, U. Weierstall, V. Panneels, E. Nango, S. Iwata, M. Hunter, I. Schapiro, G. Schertler, R. Neutze and J. Standfuss (2018). "Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser." Science 10.1126/science.aat0094Nogly-2018.

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