Tag: Chemistry

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Scientists take a freeze-frame look at excited electrons

Scientists used a pair of X-ray pulses (shown in pink and green) to study the energetic response of electrons (gold) in liquid water on attosecond time scales, while the hydrogen (white) and oxygen (red) atoms are ‘frozen’ in time. (Pacific Northwest National Laboratory / Nathan Johnson)

An international team of scientists has blazed a new trail for studying how atoms respond to radiation, by tracking the energetic movement of electrons when a sample of liquid water is blasted with X-rays.

The experiment, described in this week’s issue of the journal Science, required “freezing” the motion of the atoms with which the electrons were associated, on a scale of mere attoseconds. An attosecond is one-quintillionth of a second — or, expressed another way, a millionth of a trillionth of a second.

Attosecond-scale observations could provide scientists with new insights into how radiation exposure affects objects and people.

“What happens to an atom when it is struck by ionizing radiation, like an X-ray? Seeing the earliest stages of this process has long been a missing piece in understanding how radiation affects matter,” Xiaosong Li, a chemistry professor at the University of Washington and a laboratory fellow at the Pacific Northwest National Laboratory, said in a UW news release. “This new technique for the first time shows us that missing piece and opens the door to seeing the steps where so much complex — and interesting — chemistry occurs!”

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Scientists visit the kind of lake where life may have arisen

Researchers walk across Last Chance Lake’s crusty surface in September 2022. (UW Photo / Zack Cohen)

Several years ago, scientists at the University of Washington theorized that key ingredients for life could have built up billions of years ago in special kinds of environments known as soda lakes.

At the time, their hypothesis was based on previously published research, computer modeling and lab experiments. But now the same scientists say they’ve found a shallow lake that just might fit the requirements — and it happens to be just a few hundred miles north of their home base in Seattle.

Their findings, focusing on Last Chance Lake in British Columbia, were published this month in Communications Earth & Environment, an open-access, peer-reviewed scientific journal.

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Scientists say Saturnian moon has all of life’s essentials

A cutaway view shows water rising up from Enceladus’ ice-covered ocean. (NASA / JPL-Caltech Illustration)

Phosphorus, an essential ingredient for life as we know it, has been detected for the first time in water samples that can be traced back to Enceladus, an ice-covered moon of Saturn.

The discovery, reported today in the journal Nature, lends further support to suggestions that life could lurk within Enceladus’ ice-covered oceans — and perhaps in similar environments elsewhere in the solar system.

Phosphorus-containing compounds, known as phosphates, provide the molecular backbone for DNA and RNA molecules. Adenosine triphosphate, or ATP, serves as the source of energy for living cells. This research marks the first time that phosphates have been traced to an extraterrestrial ocean. The Nature paper suggests that phosphate levels in Enceladus’ hidden seas could be hundreds or even thousands of times higher than what exists in Earth’s oceans.

“By determining such high phosphate concentrations readily available in Enceladus’ ocean, we have now satisfied what is generally considered one of the strictest requirements in establishing whether celestial bodies are habitable,” study co-author Fabian Klenner, a postdoctoral researcher at the University of Washington, said in a news release.

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Azure Quantum joins the hunt for new fuel-cell catalysts

A hydrogen-powered car fills up at a refueling station. (Johnson Matthey via YouTube)

Chemists at Microsoft Azure Quantum are teaming up with Johnson Matthey, a British-based clean-tech company, to identify new types of catalysts for hydrogen fuel cells.

The project demonstrates how quantum information science could help reduce the automobile industry’s carbon footprint and address the challenge of climate change.

“So far, Johnson Matthey has seen a twofold acceleration in quantum chemistry calculations, and we’re just getting started,” Nathan Baker, senior director of partnerships for chemistry and materials at Microsoft, said today in a blog posting. “Both companies recognize that the discoveries needed to create a zero-carbon future will require significant breakthroughs in chemical and materials science, and are enthusiastic about the difference we can make in the world together.”

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A new type of salt crystal could exist on Europa

An image from NASA’s Galileo orbiter shows Europa’s surface of salt-streaked ice. (Credit: NASA / JPL / Ted Stryk)

A prime target in the search for extraterrestrial life is Europa, a moon of Jupiter that’s covered with a sheet of salty ice. But what kind of salt is there? Researchers say they’ve created a new kind of salt crystal that could fill the bill, and perhaps raise hopes for finding life under the ice.

This salt crystal is both exotic and common: It’s actually table salt — also known as sodium chloride, with the chemical formula NaCl — but bound up with water molecules to form a hydrate that doesn’t exist naturally on Earth.

Earthly sodium chloride hydrates are composed of one salt molecule linked by hydrogen bonds with two water molecules. In contrast, the hydrates created in the lab consist of two NaCl molecules to 17 water molecules, or one NaCl molecule to 13 water molecules. (The structure for a third type of “hyperhydrated hydrate” couldn’t be determined.)

That’s promising news for scientists who study Europa and other ice-covered worlds — including two other Jovian moons, Callisto and Ganymede; and the Saturnian moons Enceladus and Titan. Spectral observations indicate that Europa’s surface ice contains salts, including sodium chloride, but the observed levels of concentration don’t match up well with Earth’s run-of-the-mill NaCl hydrates.

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Synthetic peptide molecules open the way for new drugs

An illustration shows how peptide molecules can slip through a cell membrane. (Image by Ian C. Haydon / UW IPD)

Researchers at the University of Washington have discovered how to create peptide molecules that can slip through membranes to enter cells — and they’ve also created a company to take advantage of the discovery for drug development.

The findings, which were published today in the journal Cell, could eventually lead to new types of oral medications for health disorders ranging from COVID-19 to cancer.

“This new ability to design membrane-permeable peptides with high structural accuracy opens the door to a new class of medicines that combine the advantages of traditional small-molecule drugs and larger protein therapeutics,” senior study author David Baker, a biochemist at the University of Washington School of Medicine, said in a news release.

Small-molecule drugs — for example, aspirin — are small enough to slip through cell membranes to do their work. Protein therapeutics — for example, monoclonal antibodies — can target more complex ailments, but the protein molecules are typically too big to wedge their way through lipid-based cell walls.

Peptide drugs are made from the same building blocks as protein, and offer many of the advantages of protein-based drugs. They can bind protein targets in the body more precisely than small-molecule drugs, promising fewer side effects.

“We know that peptides can be excellent medicines, but a big problem is that they don’t get into cells,” said study lead author Gaurav Bhardwaj, an assistant professor of medicinal chemistry at the UW School of Pharmacy. “There are a lot of great drug targets inside our cells, and if we can get in there, that space opens up.”

The newly reported experiments used a couple of molecular design techniques to create types of peptide molecules that can get into cells more easily.

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Protein designers get a $45 million boost

University of Washington biochemists David Baker and Neil King show off molecular models of proteins at UW’s Institute for Protein Design. (UW IPD Photo / Ian Haydon)

The era of engineering proteins for medical applications just got a lot closer, thanks to a five-year, $45 million grant from The Audacious Project at TED to the Institute for Protein Design at the University of Washington School of Medicine.

The institute, headed by UW biochemist David Baker, is among eight recipients of Audacious grants announced today at the annual TED conference in Vancouver, B.C.

“We’re really thinking of this as a protein design revolution, parallel to the digital revolution at Bell Labs. … If you can design proteins exactly to order from first principles, you can solve a lot of problems that are facing humans today — primarily in medicine, but also in materials and energy,” Baker told GeekWire.

Among the potential products are a universal flu vaccine, non-addictive painkillers, smart proteins capable of identifying and treating cancer cells or the out-of-control cells that cause autoimmune disorders, potential treatments for neurodegenerative disorders and self-assembling proteins for solar cells or nanofabrication.

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Scientists design proteins that snap together

This molecular visualization shows how proteins are assembled like building blocks. (UW Illustration)

Researchers have created molecular building blocks that can weave themselves into long threads of protein.

Well, maybe not all that long. Each protein-based building block measures only a nanometer in length, and the self-assembled filaments get about as long as 10,000 nanometers. It’d take more than 2,500 of those filaments, laid end to end, to amount to an inch in total length. Nevertheless, the feat described in this week’s issue of the journal Science demonstrates the power and beauty of protein design.

“Being able to create protein filaments from scratch — or de novo — will help us better understand the structure and mechanics of naturally occurring protein filaments and will also allow us to create entirely novel materials, unlike any found in nature,” senior study author David Baker of the University of Washington said today in a news release.

Baker is a biochemist at the UW School of Medicine and director of UW’s Institute for Protein Design, which has pioneered the protein-folding field for years.

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Scientists fine-tune the formula for finding life

An artist’s conception shows the light of an alien star shining through a planet’s atmosphere. (NASA Goddard via YouTube)

Is the presence of oxygen in the atmosphere of an alien world the only sure-fire sign that life is present? Not necessarily: Scientists say the chemical signature of biological activity is likely to be more subtle, involving a mix of gases that might seem out of whack.

In a paper published today in Science Advances, researchers say future observatories such as NASA’s James Webb Space Telescope should look for the signature of atmospheric gases that would be in disequilibrium if it weren’t for biological processes.

The study’s lead author, Joshua Krissansen-Totton of the University of Washington, says looking for oxygen alone shouldn’t be the sole strategy in the search for life on extrasolar planets.

“This idea of looking for atmospheric oxygen as a biosignature has been around for a long time. And it’s a good strategy — it’s very hard to make much oxygen without life,” he said in a news release. “But we don’t want to put all our eggs in one basket. Even if life is common in the cosmos, we have no idea if it will be life that makes oxygen. The biochemistry of oxygen production is very complex and could be quite rare.”

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Chemistry Nobel honors super-cool micro-imaging

This year’s Nobel Prize for chemistry recognizes the invention of cryo-electron microscopy, a method for chilling down biomolecules to produce less jittery, more precise pictures of them.

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