Nine Nobel Prize Predictions for 2020
Abigail Malate, Staff Illustrator
Copyright American Institute of Physics
(Inside Science) -- Making predictions for the Nobel prizes in physiology or medicine, physics and chemistry has become an annual pastime at Inside Science. We've had some success in prior years. For example, in 2018 we included the winning research about cancer immunotherapy in our physiology or medicine predictions. We also included eventual 2019 winner lithium ion batteries in the 2018 chemistry predictions. In 2019, we correctly picked exoplanets for the physics prize. This year we've searched for hints hidden in data -- as well as relied on our nonscientific intuitions -- to make our nine best predictions for the winners of the 2020 Nobel Prizes.
To check out the research we highlighted last year that didn't win but may be recognized this year, please read our 2019 predictions.
The Nobel Prize in Physiology or Medicine -- Announced October 5
Written by Nala Rogers
The shape of the immune system's signposts
Killer T cells are immune system assassins that destroy traitorous versions of the body's own cells -- usually cells infected with viruses. By the 1980s, researchers knew that killer T cells couldn't find such traitors without the help of major histocompatibility, or "MHC," proteins, which stick out from the surfaces of cells. But it wasn't clear how MHC proteins identified the T cells' targets.
As a postdoctoral researcher in Don Wiley's Harvard laboratory, Pamela Björkman used X-ray crystallography to solve the physical structure of an MHC protein in 1987. The protein had a groove on its surface, formed by two helix-shaped structures that could clamp together like a bear trap. These helixes were already clamped around a mixture of short protein segments called peptides.
That gave the researchers the clues they needed to understand how MHC proteins work. Cells are constantly chopping old proteins into peptides as part of normal cleanup processes. These peptides get shuttled into a compartment in the cell where they meet up with MHC proteins. The MHC proteins grab the peptides, migrate out of the cell and then display their bounty to passing T cells. If a cell gets infected with a virus and starts producing more viruses, viral material will be chopped up and displayed as well, signaling that the cell should be destroyed.
The assembly that awards the prize in physiology or medicine might be hesitant to honor this research on MHC proteins, since the discovery built on earlier work by Peter Doherty and Rolf Zinkernagel that won a Nobel Prize in 1996. Still, it was profoundly important, helping to lay the foundation for our modern understanding of the cellular immune system. And this year, Björkman and her colleague Jack Strominger joined the ranks of Clarivate's "Citation Laureates," researchers thought to be Nobel candidates because their research publications have received exceptionally high numbers of citations.
Mini-organs as models
It's been scarcely more than a decade since researchers first coaxed stem cells to grow into 3D structures resembling miniature mouse intestines. These structures were composed of multiple types of tissue that organized themselves and interacted much as they do in the gut of a living mouse.
In the intervening years, various research teams have performed similar feats with human stem cells, producing "organoids" representing everything from the liver to the brain. Organoids have led to a revolution in medical research, providing a realistic alternative to the tissue cultures and lab animals traditionally used in preclinical experiments.
Organoids can be used to test how humans will react to new drugs or toxins and to study how the body interacts with beneficial microbes or disease-causing organisms. Organoids grown from a patient's own cells can help reveal which treatments that person will respond to -- a form of personalized medicine. And organoids grown from cancer cells are allowing researchers to study cancer in new ways.
If organoids were to be honored with a Nobel Prize, Hans Clevers would almost certainly be among the recipients. Clevers published one of the landmark papers on mouse intestine organoids with Toshiro Sato in 2009, and he has continued to be a leader in the field, receiving numerous awards and honors. Akifumi Ootani was also one of the first to produce organoids, publishing his technique the same year as Clevers and Sato. Yoshiki Sasai deserves recognition for developing brain organoids, but sadly he is out of the running for the Nobel, since he passed away in 2014 and the prizes are not awarded posthumously.
Histones and epigenetics
The strands of DNA in a cell's nucleus aren't crumpled up willy-nilly. They are wound around a series of structures called histones, somewhat like thread on spools.
But histones are more than a tidy storage mechanism. Research in the second half of the 20th century revealed that they help control which genes are active. Active genes are ones that are being transcribed into RNA, which can then be translated into the proteins that make up living things.
When DNA is wound tightly around histones, it is less accessible to the cellular machinery that translates it into RNA. But a variety of chemical groups can modify gene activity by binding to or detaching from histones. The first example that researchers found is how a chemical component known as an acetyl group attaches to the end of a histone, activating certain genes by loosening the histone's hold on DNA.
This discovery was a momentous advance in the budding field of epigenetics, the study of changes to genetic material that help determine the effects of genes without changing the underlying DNA sequence. Researchers have since attributed certain genetic disorders to defects in the body's ability to modify histones. Histone modifications and other epigenetic alterations may also play roles in diverse conditions ranging from schizophrenia to cancer.
Key figures in the discovery of histone acetylation include Michael Grunstein at UCLA, C. David Allis at The Rockefeller University, and Shelley Berger at the University of Pennsylvania. In 2018, Grunstein and Allis received a Lasker Award, often considered a harbinger of a possible Nobel.
The Nobel Prize in Physics -- Announced October 6
Written by Yuen Yiu
First image of a black hole
This picture of a fuzzy orange ring was a star among the biggest science stories in 2019. It was the first-ever image of a black hole, captured by the Event Horizon Telescope Collaboration, an international effort that gathers data with telescopes around the globe.
The black hole, hovering near the center of galaxy M87, is 6.5 billion times more massive than our sun. The image of the black hole, or rather the shadow of the black hole, circled by a ring of fuzzy light, marked a milestone in our ability to study the physics of perhaps the most mysterious objects in the universe.
Announced in April 2019, the feat might have missed the traditional end-of-January deadline to be nominated for the prize in 2019.
The first detection of gravitational waves faced a similar timeline, with the discovery announced Feb. 11, 2016, missing the boat for the 2016 prize. Three scientists behind the discovery -- Kip Thorne, Rainer Weiss and Barry Barish -- were promptly awarded the prize the following year, but the recognition came too late to honor Ronald Drever, who had passed away in March 2017. Drever was instrumental in developing the experimental techniques that made the detection of gravitational waves possible.
If Drever had been alive, the Nobel Committee might have had a harder time choosing which three out of the four deserving scientists should get the prize. The Committee’s insistence upon its tradition of limiting the prize to a maximum of three individuals has drawn criticisms for reinforcing the outdated idea of “lone geniuses” in science. If the 2020 award is given for the black hole photo, it is unclear who the Committee will choose.
Density functional theory
Among the most popular and versatile theories in materials science and computational physics and chemistry, density functional theory (DFT) has been pivotal in the discovery of many functional materials used in modern gadgets.
The theory is intimately related to the Schrödinger equation, which is used to describe and predict the behavior of a quantum system. However, the equation becomes exceedingly difficult to calculate for so-called many-body systems, such as a hunk of metal containing trillions upon trillions of electrons. DFT provides a way to rethink the problem and produces effective approximations for these systems, making it possible to calculate the electronic and nuclear structures of materials.
One of the pioneers of the theory, Walter Kohn, was awarded the 1998 Nobel Prize in chemistry, along with John Pople, who pioneered computational methods in quantum chemistry that allowed scientists to put theories such as DFT to use. However, given the explosive growth in materials science, particularly in relation to information technology and clean energy production, it isn’t unthinkable for the Nobel Committee to honor others who have also contributed to the development of DFT but have not yet been recognized with the prize.
Possibilities include John Perdew, whose work at multiple institutions has made him one of the most cited scientists on DFT and in physics, or Lu Jeu Sham from UC San Diego, who worked with the aforementioned Kohn on the Kohn-Sham equation, a specialized form of DFT widely used in materials science and quantum chemistry.
We have previously predicted that scientists working on quantum communication technology might get the nod from the Committee. In particular, we mentioned the trio of Alain Aspect, John Clauser and Anton Zeilinger, who were recognized by the Wolf Prize in 2010 “for their fundamental conceptual and experimental contributions to the foundations of quantum physics, specifically an increasingly sophisticated series of tests of Bell's inequalities.”
In the field of quantum information research, quantum computers have had a big year. Google and IBM appeared to be in a public spat when scientists from IBM tried to downplay Google’s audacious claim of having achieved “quantum supremacy,” a statement that made the rounds in science news outlets.
In a paper in the journal Nature, Google claims that their latest quantum computer, Sycamore, can complete a specific calculation in 200 seconds, and that the said calculation would take a supercomputer such as IBM’s Summit, 10,000 years to do. IBM shot back by saying that Summit can probably complete the calculation in closer to two and a half days. Regardless of the public relations battle, it was a significant milestone for quantum computing -- a quantum processor with only 53-qubits, the quantum equivalent of a classical bit, was able to outperform a supercomputer capable of performing 200 thousand trillion calculations per second.
Serge Haroche and David Wineland were awarded the 2012 prize, “for ground-breaking experimental methods that enable measuring and manipulation of individual quantum systems.” However, with practical applications for quantum information technologies becoming more apparent every year, the Committee may choose to shine the spotlight on the field once again. The remaining question is, who will they pick?
The Nobel Prize in Chemistry -- Announced October 7
Written by Catherine Meyers
Building new polymers, piece by piece
From plastic milk jugs to the epoxy resin that helps hold circuit boards together, synthetic polymers are everywhere in everyday lives. These highly versatile materials are made up of long strings of smaller units called monomers. Polymers can be soft and flexible, like a polyurethane dish sponge, or hard and rigid, like a Lego brick.
The 2020 Nobel Prize in chemistry may go to the scientists who invented a new way to make bespoke polymers in a highly controlled, efficient and economical fashion. In 1995, Carnegie Mellon University chemist Krzysztof Matyjaszewski and his colleague Jin-Shan Wang published a paper on a method called atom transfer radical polymerization. The method can be used to build complex polymers piece by piece with the help of a special catalyst to add monomers to a growing chain. The process can be started and stopped by controlling the temperature and other conditions of the reaction. Importantly, all of this can be accomplished using industrial equipment.
This technology has been adopted by commercial companies and used in cosmetics, printer inks, adhesives, sealants and more. Researchers continue to explore ways they can use it to make new materials with tailored properties, such as coatings for biomedical devices and degradable plastics.
The chemistry behind Moore’s Law
An average smartphone today has millions of times more memory than the computer aboard Apollo 11, which flew astronauts to the moon in 1969. This year's chemistry prize may recognize some of the creative chemical research that helped make this radical increase in computing capability possible.
The brains of modern computers are etched out of silicon chips. To make the patterns on these chips, manufacturers coat the chips with a material called a photoresist, which reacts to light. They then shine the desired patterns onto the chips. The light makes chemical changes in the photoresist that make it either easier or harder to remove the underlying material.
Making computers more powerful has typically required making the patterns on the chips smaller. In the late 1970s chip manufacturers were facing a limit -- if they wanted to make chips with finer details, they had to use a shorter wavelength of light. The problem was that light sources that produced these shorter wavelengths were too weak to be practical.
Researchers at IBM started investigating how they might make a more sensitive photoresist that would work with weaker light. They hit upon the idea of a chemical chain reaction, in which a small number of changes caused by the light would cascade into big changes in the material. Thus were born chemically amplified photoresists. It took a number of years to perfect the formulas and work out the kinks in the process, but by 1986 IBM was making chips with a record 1 megabits of memory using the new technology. Two of the main researchers who might be recognized with the prize are C. Grant Willson and Jean Fréchet. Hiroshi Ito, another key contributor, passed away in 2009.
Better tools for understanding life’s building blocks
In his book, “Imagined Worlds,” the late physicist Freeman Dyson wrote, “New directions in science are launched by new tools much more often than by new concepts. The effect of a concept-driven revolution is to explain old things in new ways. The effect of a tool-driven revolution is to discover new things that have to be explained.”
The 2020 Nobel Prize in chemistry may recognize researchers who built tools that helped launched a revolution in understanding and manipulating the chemical building blocks of life. In the 1970s and ’80s, researcher Lee Hood, who was working at Caltech at the time, and his colleagues developed machines to sequence and synthesize proteins and DNA. Hood’s key collaborators included Marvin Caruthers at the University of Colorado and Michael Hunkapiller at Caltech.
The new tools gave researchers more speed and sensitivity. They have enabled breakthroughs in the study of biology and disease and led to the development of new drugs and medical treatments. For example, the automated DNA sequencer and the more advanced machines that followed made the human genome project possible, and the protein synthesizer helped drug company Merck make a key part of the HIV virus, determine its structure and design a drug to combat the virus.
An article for the Lasker Foundation, which honored Hood in 1987 for his work on key proteins of the immune system called antibodies, noted the interdisciplinary nature of Hood’s work. He’s quoted as saying the first paradigm shift of his career was “bringing engineering to biology.” But it might be the chemistry prize that recognizes his contributions.
For more of Inside Science's coverage of the 2020 Nobel Prizes in physiology or medicine, physics and chemistry, please visit our Nobel coverage page.