Watching complex molecules at work

Time-resolved infrared spectroscopy in the sub-millisecond range is an important method for studying the relationship between function and structure in biological molecules. However, the method only works if the reaction ...

Scientists reveal the structure of viral rhodopsins

The structure of an Organic Lake Phycodnavirus rhodopsin II (OLPVRII), which is a unique protein found in the genome of giant viruses, has been determined thanks to the work of MIPT graduates and Ph.D. students. The paper ...

Expanding the optogenetics toolkit

Controlling individual brain cells using light-sensitive proteins has proven to be a powerful tool for probing the brain's complexities. As this branch of neuroscience has expanded, so has the demand for a diverse palette ...

How Chesapeake Bay bacteria snack on sunlight

The Chesapeake Bay is known for its blue crabs, but those crustaceans are far outnumbered by much tinier residents: bacteria. Every milliliter of bay water is home to thousands to millions of these marine microbes, critical ...

Rhodopsin on track: Biological pigment aligns in double rows

Scientists from the caesar research center, an Institute of the Max Planck Society, have explained, with the help of electron microscopy, how the pigment rhodopsin is arranged in the rod cells of the retina. This question ...

Researchers model potential of toxic algae photoreceptors

Blue-green algae is causing havoc in Midwestern lakes saturated with agricultural run-off, but researchers in a northwest Ohio lab are using supercomputers to study a closely related strain of the toxic cyanobacteria to harness ...

Light-sensing receptor plays role in temperature sensation: study

A light-sensing receptor that's packed inside the eye's photoreceptor cells has an altogether surprising role in cells elsewhere in the body, Johns Hopkins scientists have discovered. Using fruit flies, they showed that this ...

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