Professor Bernard Feringa speaks at the University of Groningen on October 5, 2016 after receiving the 2016 Nobel Chemistry Prize, along with two other scientists.
Machines do work. They toil against equilibrium, entropy, death. And since the Industrial Revolution, machines have become ubiquitous, a practically invisible backdrop to the macroscopic world. This year’s Nobel Prize for chemistry goes to scientists who did foundational work in making machines part of the nano-scale world—that is, actually invisible.
Molecules are governed by random rules, and naturally edge towards equilibrium. They are also impossible to manipulate without using chemistry. This year’s winners—Jean-Pierre Sauvage, Sir James Fraser Stoddart, and Bernard Feringa—used chemical attractions and cohesions to construct molecular chains, axles, motors, muscles, and even computer chips. These discoveries could someday lead to awesome new materials, sensors, and batteries.
Richard Feynman predicted nanoscale machines during a 1984 lecture. Actually, he was a little late. A year earlier, Sauvage, a chemist at the University of Strasbourg in France, had figured out a way to mass-produce molecular chains. Chains are one of the simplest types of machine. But nanochemists had spent decades searching for a simple way to get one ringed molecule to link with another. Sauvage solved the problem by placing a copper atom inside a ringed molecule, then introducing a crescent shaped molecule nearby. The copper atom attracted the crescent into the ring’s hole. Then add another crescent, and use a chemical reaction to bond the two crescents into a single ring. Sauvage’s method dramatically increased the yield of these nanoscale chains, called catenanes.
Stoddard, of Northwestern University, made the next big contributions beginning in 1994. He threaded a molecular ring around an axle, creating the teeniest wheel. This little machine, called a rotaxane, formed the basis of more complicated nanoscale machines, including: a lift capable of moving 0.7 nanometers; a pair of threaded loops that contract and extend like a muscle; and tiny transistors on a nanoscale computer chip capable of storing 20 kilobytes of memory.
Muscles and computer chips are pretty awesome, but all of them require some kind of meddling to make them do work. Motors are machines that make other machines do work, and they were the next big goal for nanomachinists. The problem is, motors need to convert the energy they ingest into motion in a constant direction. Molecules love equilibrium, though. Put some energy in one and it’s just as likely to spin one way as the other.
In 1999, at the University of Groningen in the Netherlands, Feringa used chemistry techniques to engineer his way around the equilibrium problem. First, he made a molecule out of two flat chemical structures, joined with carbon atoms. These structures were like rotor blades. He then attached methyl groups—three hydrogen atoms and one carbon atom—to the rotors. Then, Feringa exposed the structure to ultraviolet light. One of the rotors would jump 180 degrees around the central carbon bond, and the two methyl groups were now facing each other. Another flash of UV forced the other rotor blade to jump. Again, the methyl groups prevented the rotors from moving backwards. Equilibrium interrupted.
Feringa has kept up his nanomotor work. In 2011 he and his lab built at molecular car. By 2014, they had build a nanomotor capable of 12 million rotations per second. Just imagine: Someday, intelligent viruses might use nanoscopic hot rods to do burnouts while evading your body’s buzzkill immune response. And for the home team, microscopic mech suits for your white blood cells.
John Michael Kosterlitz, one of the three Nobel Prize recipients in Physics, at Aalto University on October 4, 2016.
A physicist walks into a room holding a pretzel, a bagel, and a cinnamon bun. “For us, these are very different. This one’s sweet, this one’s salty, they have different shapes,” says the physicist. “But, if you’re a topologist there’s only one thing that’s really interesting: This thing has no hole, the bagel has one hole, the pretzel has two holes.” Haha, get it!?
Sigh. The pastry thing was Nobel committee member Thors Hans Hansson’s best attempt to explain topology, the core concept behind the winner of this year’s prize for physics, “for theoretical discoveries of topological phase transitions and topological phases of matter.” Basically this has to do with a bunch of theoretical work that looked at how you make superconductors, superfluids, and super-thin magnets by super-chilling or super-condensing matter. This super-theoretical work is the foundation for super-new materials that might one day replace wires and parts in future supercomputers.
Three scientists split the award: David Thouless of the University of Washington; Duncan Haldane of Princeton University; and Michael Kosterlitz of Brown University. Thouless will get half of of the $937,000 prize money, and Haldane and Kosterlitz will split the other half.
These three did their Nobel-worthy theoretical work in the 1970s and ’80s. Kosterlitz and Thouless’ work came first, when they proved—contrary to the prevailing understanding—that super-thin layers of matter could act as superconductors or superfluids. They also figured out why the temperature of superconducting materials matters: These materials changed phase slightly when warmed up. Haldane’s contribution also came in the ’80s, using topology to describe properties of tiny magnets. Thouless also did some additional Nobel-worthy work, around the same time as Haldane, by figuring out that electricity passed through thin, superconducting materials in precise integer steps.
Topology has grown into a robust sub-discipline in physics, where scientists use these concepts to develop new types of materials for computing, electrical transmission, and battery storage. Someday, materials based on these winners’ theoretical work might power Siri’s quantum-brained sass.
And to the Nobel committee: Maybe next time you bring a bunch of pastries on stage, have a better punch line. Also, how about an award for bagels? Because, come on, somebody deserves an award for bagels.
Yoshinori Ohsumi attends a press conference on October 3, 2016 in Tokyo, Japan.
The 2016 Nobel Prize for Physiology or Medicine goes to the discovery that … wait for it … your body is eating itself. Autophagy, fully described in the 1990s by Japanese biologist Yoshinori Ohsumi, is how cells recycle damaged, diseased, or worn-out bits of microscopic machinery into new, fully functional organic stuff.
Autophagy is a crucial part of your health. Whether through physical trauma, infection, or just age, your cells are constantly getting damaged. Without this biological recycling process, your body would quickly clutter up with busted-down cellular parts. Diseases like Parkinson’s and some types of cancer are caused when autophagy breaks down. It’s also how humans survive starvation, because it allows the body to cannibalize itself for energy.
Biologists have known that cells recycle themselves for a while. But Ohsumi’s work in the 1990s—while he was a junior researcher at the University of Tokyo—identified the genes and metabolic pathways that trigger autophagy. His pioneering work opened up a whole new branch of biology looking into how bodies use (or fail to use) self-cannibalization to stay healthy.
In addition to international acclaim, Sweden’s Karolinksa Institute awarded Ohsumi nearly $1 million for his discovery on Monday, October 3. The institute will announce the Nobel Prize in Physics on October 4, and Chemistry on October 5.
The chemists aren’t going to be happy about this one. Over the last decade, the Nobel Prize in Chemistry has often gone to biochemistry, which to chemists is only sort-of real science. And this year’s prize, announced today, is no exception.
The winners: three scientists who parsed the molecular mechanisms that drive the repair of damaged DNA. The stuff of genetic code, the long chains of bases that are the chemical blueprints of life, doesn’t just stay filed away in some cellular safe deposit box. Even when cellular machinery isn’t reading it to make proteins—that’s what genes are for—DNA is dynamic, copying itself when cells divide. And living things have so much DNA, getting copied so many times, that the system is bound to mess up a letter here or there. It’s also constantly under assault from environmental mutagens like radiation and free radicals.
Those mistakes, sadly, don’t turn you into an X-Man. In fact, one of today’s laureates, Tomas Lindahl, discovered just how big of a problem those built-up errors really are. Genetic information decays, and the mistakes add up fast enough that without built-in repair mechanisms, humans wouldn’t be here. Evolution itself would break. After realizing that, Lindahl figured out one of the repair systems: base excision repair, in which an assembly of proteins slices an erroneous base out of a stretch of DNA and replaces it with the right one.
Those single-base errors usually occur spontaneously. But another mechanism of DNA repair, nucleotide excision (discovered by Aziz Sancar), targets more extensive genetic damage caused by UV radiation. (When the system fails, you can end up with skin cancer.) The third recipient of the prize, Paul Modrich, discovered how cells correct errors introduced during DNA copying. When that mismatch repair system goes haywire, people can end up with colon cancer.
All of those discoveries are essential biochemical knowledge—they’re happening in your body right now, and if you’re really quiet, you might be able to hear them. (Not really.) But in the end, thanks to their carcinogenic connections, they may have just as much influence in medicine as in chemistry. Time for a new classification scheme, Stockholm?
It’s really hard to pick who should get Nobel Prizes for work in physics. New discoveries in the field tend to come from massive international collaborations of physicists running multimillion-dollar experiments in huge particle accelerators and super-sensitive detectors. And indeed, that’s who today’s 2015 physics Nobel went to: two of those huge projects, by way of their leading physicists.
This year, the Nobel committee honors the ongoing quest to understand the subatomic particle called a neutrino, the second-most abundant particle in the universe…and the most elusive. Neutrinos come in three flavors—tau, electron, and muon—and none of them interact much with normal matter. Which makes detecting and studying them a wee bit difficult.
That’s what makes the work of the two physicists, Takaaki Kajita and Arthur B. McDonald, so cool. Working at two different neutrino observatories, they built experiments to pick out the evanescent signatures of neutrinos and catch them in the act of transforming from one flavor to another.
Kajita worked on spotting those so-called neutrino oscillations at the Super-Kamiokande detector in Japan, perhaps the best-named facility in all of science. It’s also one of the nuttiest-looking physics experiments you could imagine, a 13-million gallon steel water tank buried nearly a mile beneath a mountain, lined with photomultiplier tubes that detect light produced when neutrinos interact with the water. Around the turn of the century, Kajita and his colleagues recorded evidence of neutrinos changing identities during the 183-mile journey from the proton accelerator lab in Tokai that generated them to the detector.
Around the same time, McDonald and his colleagues found evidence that neutrinos from the Sun—not human-generated ones, like those detected at Super-Kamiokande—also changed identity as they traveled to their detector at the Sudbury Neutrino Observatory in Canada, another water-filled vessel surrounded by photomultiplier tubes.
Both of those results flipped the field of physics on its head. Before their work, most researchers assumed that neutrinos had no mass—primarily because they pass like ghosts through matter and seem to move near the speed of light. The Standard Model of physics—you know, the fundamental underpinnings of physics’ understanding of matter and its behavior—requires that neutrinos be massless. But the numbers say that if they oscillate, they have mass. So something in the model is off.
That might sound like a funny thing to award nearly $1 million for, but physicists love it when something in the Standard Model is off. It gives them something to do. Any time anyone pokes a hole in the Standard Model, it’s an opportunity to find new physics—new rules to govern the universe. And continued work at the dozens of neutrino observatories around the world is still trying to nail those rules down.
Today, the Nobel committee kicked off its 2015 season by awarding the Nobel Prize in Physiology or Medicine to three scientists for the discovery of two anti-parasitic therapies—treatments that have had a direct, life-saving impact on global health.
Thomson Reuters last week predicted that the winner would have done work on a complex biochemical pathway—making connections between the gut microbiome and obesity, for example, or teasing apart the role of T cells in autoimmune illnesses. But today’s winners had a simpler, if no less difficult, goal: to identify, among thousands of bacterial cultures and herbal extracts, the ones with promise as parasite-killing drugs. It’s a reminder that many of medicine’s most effective therapies aren’t designed, but discovered.
Two of today’s winners, William C. Campbell and Satoshi Ōmura, came up with a drug to fight infections from roundworms—conditions like river blindness and lymphatic filariasis that affect a third of the world’s population. Ōmura sifted through huge repositories of soil bacteria, finding 50 strains of Streptomyces with potential anti-parasitic activity; Campbell isolated a compound, avermectin, from one of them. Campbell’s team further modified avermectin into an even more effective drug called ivermectin—the beginning of a whole new class of anti-parasitics.
The other half of the $900,000 award went to a primary drug to treat malaria. Youyou Tu discovered artemisinin by screening herbal remedies; she found a compound in Artemisia annua, or sweet wormwood, that kills malaria parasites. The disease still kills about half a million people a year, but artemisinin therapy has reduced that annual figure by about 100,000. Ivermectin has protected millions of people against parasitic disease; both drugs have been crucial additions to medicine’s ongoing game of anti-parasitic whack-a-mole.