Duke Research Blog

Following the people and events that make up the research community at Duke.

Author: Kara Manke (Page 1 of 3)

Cheating Time to Watch Liquids do the Slow Dance

Colorful spheres simulating liquid molecules shift around inside a cube shape

The team’s new algorithm is able to simulate molecular configurations of supercooled liquids below the glass transition. The properties of these configurations are helping to solve a 70-year paradox about the entropy of glasses. Credit: Misaki Ozawa and Andrea Ninarello, Université de Montpellier.

If you could put on a pair of swimming goggles, shrink yourself down like a character from The Magic School Bus and take a deep dive inside a liquid, you would see a crowd of molecules all partying like it’s 1999.

All this frenetic wiggling makes it easy for molecules to rearrange themselves and for the liquid as a whole to change shape. But for supercooled liquids — liquids like honey that are cooled below their freezing point without crystallizing – the lower temperature slows down the dancing like Etta James’ “At Last.” Lower the temperature enough, and the slow-down can be so dramatic that it takes centuries or even millennia for the molecules to rearrange and the liquid to move.

Scientists can’t study processes that last longer than their careers. But Duke chemists and their Simons Foundation collaborators have found a way to cheat time, simulating the slow dance of deeply supercooled liquids. Along the way, they have found new physical properties of “aged” supercooled liquids and glasses.

A droplet rises above a surface of water

Credit: Ruben Alexander via Flickr.

To understand just how slow deeply supercooled liquids move, consider the world’s longest-running experiment, the University of Queensland’s Pitch Drop Experiment. A single drop of pitch forms every eight to thirteen years — and this pitch is moving faster than deeply supercooled liquids.

“Experimentally there is a limit to what you can observe, because even if you managed to do it over your entire career, that is still a maximum of 50 years,” said Patrick Charbonneau, an associate professor of chemistry and physics at Duke. “For many people that was considered a hard glass ceiling, beyond which you couldn’t study the behavior of supercooled liquids.”

Charbonneau, who is an expert on numerical simulations, said that using computers to simulate the behavior of supercooled liquids has even steeper time limitations. He estimates that, given the current rate of computer advancement, it would take 50 to 100 years before computers would be powerful enough for simulations to exceed experimental capabilities – and even then the simulations would take months.

To break this glass ceiling, the Charbonneau group collaborated with Ludovic Berthier and his team, who were developing an algorithm to bypass these time constraints. Rather than taking months or years to simulate how each molecule in a supercooled liquids jiggles around until the molecules rearrange, the algorithm picks individual molecules to swap places with each other, creating new molecular configurations.

This allows the team to explore new configurations that could take millennia to form naturally. These “deeply supercooled liquids and ultra-aged glasses” liquids are at a lower energy, and more stable, than any observed before.

“We were cheating time in the sense that we didn’t have to follow the dynamics of the system,” Charbonneau said. “We were able to simulate deeply supercooled liquids well beyond is possible in experiments, and it opened up a lot of possibilities.”

Two columns of blue and red spheres represent simulations of vapor-deposited glasses.

Glasses that are grown one layer at a time have a much different structure than bulk glasses. The team used their new algorithm to study how molecules in these glasses rearrange, and found that at low temperatures (right), only the molecules at the surface are mobile. The results may be used to design better types of glass for drug delivery or protective coatings. Credit: Elijah Flenner.

Last summer, the team used this technique to discover a new phase transition in low-temperature glasses. They recently published two additional studies, one of which sheds light on the “Kauzmann paradox,” a 70-year question about the entropy of supercooled liquids below the glass transition. The second explores the formation of vapor-deposited glasses, which have applications in drug delivery and protective coatings.

“Nature has only one way to equilibrate, by just following the molecular dynamics,” said Sho Yaida, a postdoctoral fellow in Charbonneau’s lab. “But the great thing about numerical simulations is you can tweak the algorithm to accelerate your experiment.”

Configurational entropy measurements in extremely supercooled liquids that break the glass ceiling.” Ludovic Berthier, Patrick Charbonneau, Daniele Coslovich, Andrea Ninarello, Misaki Ozawa and Sho Yaida. PNAS, Oct. 24, 2017. DOI: 10.1073/pnas.1706860114

The origin of ultrastability in vapor-deposited glasses.” Ludovic Berthier, Patrick Charbonneau, Elijah Flenner and Francesco Zamponi. PRL, Nov. 1, 2017. DOI: 10.1103/PhysRevLett.119.188002

Post by Kara Manke

Designing Drugs Aimed at a Different Part of Life’s Code

Individual RNA molecules fluoresce inside a breast cancer cell.

Individual RNA molecules fluoresce inside a breast cancer cell. Credit: Sunjong Kwon, Oregon Health & Science University, via Flickr.

Most drugs work by tinkering with the behavior of proteins. Like meddlesome coworkers, these molecules are designed to latch onto their target proteins and keep them from doing what they need to do.

If a protein is responsible for speeding up a reaction, the drug helps slow the reaction down. If a protein serves as a gatekeeper to a cell, regulating what gets in and what stays out, a drug changes how many molecules it lets through.

But proteins aren’t the only doers and shakers in our bodies. Scientists are finding that strings of RNA — known primarily for their role in shuttling genetic information from nucleus-bound DNA to the cell’s protein-manufacturing machinery — can also play a major role in regulating disease.

A portrait of Amanda Hargrove

Amanda Hargrove is an assistant professor of chemistry at Duke University.

“There has been what some people are calling an RNA revolution,” said Amanda Hargrove, assistant professor of chemistry at Duke. “In some diseases, non-coding RNAs, or RNAs that don’t turn into protein, seem to be the best predictors of disease, and even to be driving the disease.”

Hargrove and her team at Duke are working to design new types of drugs that target RNA rather than proteins. RNA-targeted drug molecules have the potential help treat diseases like prostate cancer and HIV, but finding them is no easy task. Most drugs have been designed to interfere with proteins, and just don’t have the same effects on RNA.

Part of the problem is that proteins and RNA have many fundamental differences, Hargrove said. While proteins are made of strings of twenty amino acids that can twist into myriad different shapes, RNA is made of strings of only four bases — adenine, guanine, cytosine and uracil.

“People have been screening drugs for different kinds of RNA for quite a while, and historically have not had a lot of success,” Hargrove said. “This begged the question, since RNA has such chemically different properties than proteins, is there something different about the small molecules that we need in order to target RNA?”

To find out, graduate student Brittany Morgan and research associate Jordan Forte combed the scientific literature to identify 104 small molecules that are known interact with specific types of RNA. They then analyzed 20 different properties of these molecules, and compared their properties to those of collections of drug molecules known to interact with proteins.

The team found significant differences in shape, atomic composition, and charge between the RNA-active molecules and the protein-active molecules. They plan to use the results to compile a collection of molecules, called a library, that are chosen to better “speak the language” of the RNA-active molecules. They hope this collection of molecules will be more likely to interact with RNA in therapeutically beneficial ways.

“We found that there are differences between the RNA-targeted molecules and the protein-targeted drugs, and some of them are pretty striking,” Hargrove said. “What that means is that we could start to enrich our screening libraries with these types of molecules, and make these types of molecules, to have better luck at targeting RNA.”

Discovery of Key Physicochemical, Structural, and Spatial Properties of RNA-Targeted Bioactive Ligands.” Brittany S. Morgan, Jordan E. Forte, Rebecca N. Culver, Yuqi Zhang and Amanda Hargrove. Angewandte Chemie, Sept. 18, 2017. DOI: 10.1002/anie.201707641

Kara J. Manke, PhDPost by Kara Manke

Lab-Made Protein Chomps Co-Factor Like a Big Ol' Gator

A protein is illustrated to look like an alligator mouth

The synthetic protein clamps down on the porphyrin like the jaws of an alligator. Credit: Nicholas Polizzi.

Proteins have the power to turbo-charge biochemical reactions inside the body.

Without the help of types of proteins called enzymes, the reaction that builds DNA could take over 130,000 years to complete. Enzymes cut that time down to just a few milliseconds.

To rev up chemical reactions, many proteins team up with smaller molecules or metals called cofactors. Chemists would like to design proteins that bind to non-biological cofactors in order to speed up chemical reactions not found in nature. But first, they have to figure out how to create man-made proteins that attach to new cofactors in exactly the right way, and that is no easy feat.

A team of chemists at Duke and UC San Francisco is the first to solve this protein design puzzle. The team created a synthetic protein that tightly binds a non-biological catalyst, a type of molecule called porphyrin that is capable of stealing electrons from other molecules when it absorbs light.

“To be able to combine man-made catalysts with proteins would be really big in the chemistry field because then you could combine the power of an enzyme with that of a reaction that isn’t found in nature,” said former Duke graduate student Nicholas Polizzi, who is now a postdoctoral researcher in William DeGrado’s lab at UCSF.

“We were able to figure out the design criteria necessary to place that porphyrin in a protein to within a very high accuracy,” Polizzi said. “That was a really big stepping stone to be able to design new protein-cofactor combinations not seen in nature.”

Proteins are made of chains of hundreds or thousands of smaller amino acids that twist and loop into complex 3-D shapes that can interlock with other molecules like pieces of a jigsaw puzzle. To catalyze chemical reactions, protein-cofactor combinations hold two or more molecules in precisely-shaped pockets that keep the molecules in just the right positions, and provide the right environment, for a chemical reaction to occur.

An illustration of a protein jigsaw puzzle

Chemists at Duke and UCSF designed a synthetic protein that tightly binds a non-biological molecule. Credit: Nicholas Polizzi.

Millions of years of evolution have created proteins that fold into the shapes that tightly grip specific cofactors and provide the perfect environments to catalyze chemical reactions.

For over 25 years, chemists have used what they know about protein folding to design synthetic amino acid sequences that twist up into useful shapes. But so far, they have been unable to design a protein that binds a non-biological cofactor with the precision necessary to power complex new chemical reactions.

Polizzi said this may be because these designs focused primarily on the “binding site” where cofactors and reacting molecules fit into the protein, while ignoring the rest of the structure. “What I did differently is that I considered essentially the entire interior of protein as the binding site for the porphyrin, as opposed to just a few amino acids that touch the porphyrin,” Polizzi said.

To understand how this works, you can think of the protein as the mouth of an alligator, said Michael Therien, William R. Kenan Jr. Professor of Chemistry at Duke. The protein latches onto a cofactor in the same way that an alligator uses its front teeth to chomp down on dinner. But for the front teeth to get a strong grip, the jaw and back teeth also have to be designed correctly.

“The new concept here is that the non-binding region of the protein is held in a shape that allows the binding region to work,” Therien said.

“We called the protein ‘gator’ in the lab,” Polizzi said.

The jaws of the gator protein actually clamp down so hard on the porphyrin cofactor that the whole structure is too rigid to catalyze a reaction, Polizzi said. But with a few tweaks to loosen up the structure, he thinks he can get it to work.

“In this reaction, often times you need a little bit of wiggle room in the protein for it to move. And there was no wiggle room in our protein, everything fit too perfectly,” Polizzi said.

CITATION: “De novo design of a hyperstable non-natural protein-ligand complex with sub-A accuracy.” Nicholas F. Polizzi, Yibing Wu, Thomas Lemmin, Alison M. Maxwell, Shao-Qing Zhang, Jeff Rawson, David N. Beratan, Michael J. Therien and William F. DeGrado. Nature Chemistry, Aug. 21, 2017. DOI: 10.1038/nchem.2846

Kara J. Manke, PhDPost by Kara Manke

Durham Traffic Data Reveal Clues to Safer Streets

Ghost bikes are a haunting site. The white-painted bicycles, often decorated with flowers or photographs, mark the locations where cyclists have been hit and killed on the street.

A white-painted bike next to a street.

A Ghost Bike located in Chapel Hill, NC.

Four of these memorials currently line the streets of Durham, and the statistics on non-fatal crashes in the community are equally sobering. According to data gathered by the North Carolina Department of Transportation, Durham county averaged 23 bicycle and 116 pedestrian crashes per year between 2011 and 2015.

But a team of Duke researchers say these grim crash data may also reveal clues for how to make Durham’s streets safer for bikers, walkers, and drivers.

This summer, a team of Duke students partnered with Durham’s Department of Transportation to analyze and map pedestrian, bicycle and motor vehicle crash data as part of the 10-week Data+ summer research program.

In the Ghost Bikes project, the team created an interactive website that allows users to explore how different factors such as the time-of-day, weather conditions, and sociodemographics affect crash risk. Insights from the data also allowed the team to develop policy recommendations for improving the safety of Durham’s streets.

“Ideally this could help make things safer, help people stay out of hospitals and save lives,” said Lauren Fox, a Duke cultural anthropology major who graduated this spring, and a member of the DATA+ Ghost Bikes team.

A map of Durham county with dots showing the locations of bicycle crashes

A heat map from the team’s interactive website shows areas with the highest density of bicycle crashes, overlaid with the locations of individual bicycle crashes.

The final analysis showed some surprising trends.

“For pedestrians the most common crash isn’t actually happening at intersections, it is happening at what is called mid-block crossings, which happen when someone is crossing in the middle of the road,” Fox said.

To mitigate the risks, the team’s Executive Summary includes recommendations to install crosswalks, median islands and bike lanes to roads with a high density of crashes.

They also found that males, who make up about two-thirds of bicycle commuters over the age of 16, are involved in 75% of bicycle crashes.

“We found that male cyclists over age 16 actually are hit at a statistically higher rate,” said Elizabeth Ratliff, a junior majoring in statistical science. “But we don’t know why. We don’t know if this is because males are riskier bikers, if it is because they are physically bigger objects to hit, or if it just happens to be a statistical coincidence of a very unlikely nature.”

To build their website, the team integrated more than 20 sets of crash data from a wide variety of different sources, including city, county, regional and state reports, and in an array of formats, from maps to Excel spreadsheets.

“They had to fit together many different data sources that don’t necessarily speak to each other,” said faculty advisor Harris Solomon, an associate professor of cultural anthropology and global health at Duke.  The Ghost Bikes project arose out of Solomon’s research on traffic accidents in India, supported by the National Science Foundation Cultural Anthropology Program.

In Solomon’s Spring 2017 anthropology and global health seminar, students explored the role of the ghost bikes as memorials in the Durham community. The Data+ team approached the same issues from a more quantitative angle, Solomon said.

“The bikes are a very concrete reminder that the data are about lives and deaths,” Solomon said. “By visiting the bikes, the team was able to think about the very human aspects of data work.”

“I was surprised to see how many stakeholders there are in biking,” Fox said. For example, she added, the simple act of adding a bike lane requires balancing the needs of bicyclists, nearby residents concerned with home values or parking spots, and buses or ambulances who require access to the road.

“I hadn’t seen policy work that closely in my classes, so it was interesting to see that there aren’t really simple solutions,” Fox said.

[youtube https://www.youtube.com/watch?v=YHIRqhdb7YQ&w=629&h=354]

 

Data+ is sponsored by Bass Connections, the Information Initiative at Duke, the Social Science Research Institute, the departments of Mathematics and Statistical Science and MEDx.

Other Duke sponsors include DTECH, Duke Health, Sanford School of Public Policy, Nicholas School of the Environment, Development and Alumni Affairs, Energy Initiative, Franklin Humanities Institute, Duke Institute for Brain Sciences, Office for Information Technology and the Office of the Provost, as well as the departments of Electrical & Computer Engineering, Computer Science, Biomedical Engineering, Biostatistics & Bioinformatics and Biology.

Government funding comes from the National Science Foundation. Outside funding comes from Accenture, Academic Analytics, Counter Tools and an anonymous donation.

Community partnerships, data and interesting problems come from the Durham Police Department, Durham Neighborhood Compass, Cary Institute of Ecosystem Studies, Duke Marine Lab, Center for Child and Family Policy, Northeast Ohio Medical University, TD Bank, Epsilon, Duke School of Nursing, University of Southern California, Durham Bicycle and Pedestrian Advisory Commission, Duke Surgery, MyHealth Teams, North Carolina Museum of Art and Scholars@Duke.

Writing by Kara Manke; video by Lauren Mueller and Summer Dunsmore

Not Your Basic Bench: Zebrafish Reveal Secrets of the Developing Gut

Our intestine is a highly complex organ – a tortuous, rugged channel built of many specialized cell-types and coated with a protective, slimy matrix. Yet the intestine begins as a simple tube consisting of a central lumen lined by a sheet of epithelial cells, which are smooth cells that lie on the surface of the lumen. These intestinal epithelial cells are central players in many human diseases.

A portrait of Daniel Levic

Daniel Levic, a postdoctoral research associate in the department of cell biology at the Duke University Medical Center.

Daniel Levic of the Bagnat Lab is using zebrafish as experimental models to understand how intestines are formed in hopes of finding new ways to combat disease. He wants to learn how the intestinal lumen forms during early development, and how intestinal epithelial cells take on their physiological functions.

Levic, a postdoctoral research associate in the department of cell biology at the Duke University Medical Center, focuses on projects in both basic and translational science. Daniel uses zebrafish to analyze the formation of the lumen and the polarity of epithelial cells — how specialized they are for carrying out different functions —  at the genetic and cellular level. He focuses on how membrane proteins are sorted into different, specialized domains of the cell surface and how this process affects intestinal formation. Additionally, Daniel studies how inflammation is evaded in intestinal epithelial cells in Crohn’s disease using a combination of patient biopsy samples and animal studies in zebrafish. This project is a collaborative effort aided by clinicians and human geneticists at the Duke University Medical Center.

A microscope image of a zebrafish gut

The developing gut of a zebrafish, magnified.

Though complex human diseases can’t be fully mimicked in animal models like zebrafish, this type of research can be extremely useful. These model organisms can be used to study the basic, fundamental cellular mechanisms that ultimately underlie disease. An example is Daniel’s work on Crohn’s disease, where he is trying to understand how inflammatory signaling networks become activated, specifically in intestinal epithelial cells. This problem is difficult, if not impossible, to address using exclusively human biopsy samples.

Overall, Daniel hopes that his translational research will provide new knowledge of the role of intestinal epithelial cells in Crohn’s disease and provide biomarkers that will aid clinicians in predicting how patients will respond to therapeutic interventions. Daniel’s research and basic science research are rapidly changing the way we diagnose disease, treat patients, and interact with the world around us.

Guest post by Vaishnavi Siripurapu

From Solid to Liquid and Back Again

A black and white moving image of a ball being pulled out from under a pile of circular discs

Force chains erupt as an “intruder” is yanked from beneath a pile of circular discs, which are designed to simulate a granular material. The entire process takes less than one second. Credit: Yue Zhang, Duke University.

You can easily walk across the sand on a beach. But step into a ball pit, and chances are you’ll fall right through.

Sand and ball pits are both granular materials, or materials that are made of collections of much smaller particles or grains. Depending on their density and how much force they experience, granular materials sometimes behave like liquids — something you fall right through — and sometimes “jam” into solids, making them something you can stand on.

“In some cases, these little particles have figured out how to actually form solid-like structures,” said Robert P. Behringer, James B. Duke Professor of Physics. “So why don’t they always just go squirting sideways and relax all the stress?”

Physicists do not yet understand exactly when and how jamming occurs, but Behringer’s team at Duke is on the case. The group squishes, stretches, hits, and pulls at granular materials to get a better picture of how and why they behave like they do. The team recently presented a whopping 10 papers at the 2017 Powders and Grains Conference, which occurred from July 3-7, 2017 in Montpellier, France.

Many of these studies use one of the lab’s favorite techniques, which is to create granular materials from small transparent discs that are about half an inch to an inch in diameter. These discs are made of a material which, thanks to the special way it interacts with light, changes color when squished. This effect allows the team to watch how the stress within the material changes as various forces are applied.

A blue and green moving image of spinning discs

As the wheels turn, shear strain between the discs creates a dense web of inter-particle forces. Credit: Yiqiu Zhao, Duke University.

In one experiment, graduate student Yue Zhang used a high-speed camera to catch the stress patterns as a ball on a string is yanked out from a pile of these discs. In the video, the ball first appears to be stuck under the pile, and then suddenly gives way after enough force is applied — not unlike what you might experience pulling a tent stake out of the ground, or opening the lid on a pesky pickle jar.

“The amusing thing is that you start trying to pull, you add more force, you add more force, and then at some point you pull so hard that you hit yourself in the head,” Behringer said.

The team was surprised to find that the stress patterns created by the ball, which Behringer says look “like hair all standing on end,” are almost identical to the stress of impact, only in reverse.

“What you see is even though you are just gradually gradually pulling harder and harder, the final dynamics are in some sense the same dynamics that you get on impact,” Behringer said.

In another experiment, the team examined what happens in granular materials under shear strain, which is similar to the force your fingers exert on one another when you rub them together.

Graduate student Yiqiu Zhao placed hundreds of these discs onto a circular platform made of a series of flat, concentric rings, each of which is controlled by a separate motor. As the rings turn at different speeds, the particles rub against one another, creating a shear stress.

An image of an experimental set up in a lab

Beneath the small transparent discs lie a series of concentric wheels, each attached to its own motor. By turning these platforms at different speeds, Yiqiu Zhao can observe how shear strain affects the discs.

“We have about twenty stepper motors here, so that we can rotate all the rings to apply a shear not only from the outside boundary, but also from everywhere inside the bulk of the material,” Zhao said. This ensures that each particle in the circle experiences a similar amount of shear.

“One of the key intents of this new experiment was to find a way that we could shear until the cows come home,” Behringer said. “And if it takes a hundred times more shear than I could get with older experiments, well we’ll get it.”

As the rings turn, videos of the material show forces snaking out from the inner circle like lightning bolts. They found that by applying enough shear, it is possible to make the material like a solid at much lower densities than had been seen before.

“You can actually turn a granular fluid into a granular solid by shearing it,” Behringer said. “So it is like you don’t put your ice in the refrigerator, you put it in one of these trays and you shear the tray and it turns into ice.”

Kara J. Manke, PhDPost by Kara Manke

3D Virus Cam Catches Germs Red-Handed

A 3D plot of a virus wiggling around

The Duke team used their 3D virus cam to spy on this small lentivirus as it danced through a salt water solution.

Before germs like viruses can make you sick, they first have to make a landing on one of your cells — Mars Rover style — and then punch their way inside.

A team of physical chemists at Duke is building a microscope so powerful that it can spot these minuscule germs in the act of infection.

The team has created a new 3D “virus cam” that can spy on tiny viral germs as they wriggle around in real time. In a video caught by the microscope, you can watch as a lentivirus bounces and jitters through an area a little wider that a human hair.

Next, they hope to develop this technique into a multi-functional “magic camera” that will let them see not only the dancing viruses, but also the much larger cell membranes they are trying breech.

“Really what we are trying to investigate is the very first contacts of the virus with the cell surface — how it calls receptors, and how it sheds its envelope,” said group leader Kevin Welsher, assistant professor of chemistry at Duke. “We want to watch that process in real time, and to do that, we need to be able to lock on to the virus right from the first moment.”

A 3D plot spells out the name "Duke"

To test out the microscope, the team attached a fluorescent bead to a motion controller and tracked its movements as it spelled out a familiar name.

This isn’t the first microscope that can track real-time, 3D motions of individual particles. In fact, as a postdoctoral researcher at Princeton, Welsher built an earlier model and used it to track a bright fluorescent bead as it gets stuck in the membrane of a cell.

But the new virus cam, built by Duke postdoc Shangguo Hou, can track particles that are faster-moving and dimmer compared to earlier microscopes. “We were trying to overcome a speed limit, and we were trying to do so with the fewest number of photons collected possible,” Welsher said.

The ability to spot dimmer particles is particularly important when tracking viruses, Welsher said. These small bundles of proteins and DNA don’t naturally give off any light, so to see them under a microscope, researchers first have to stick something fluorescent on them. But many bright fluorescent particles, such as quantum dots, are pretty big compared to the size of most viruses. Attaching one is kind of like sticking a baseball onto a basketball – there is a good chance it might affect how the virus moves and interacts with cells.

The new microscope can detect the fainter light given off by much smaller fluorescent proteins – which, if the virus is a basketball, are approximately the size of a pea. Fluorescent proteins can also be inserted to the viral genome, which allows them to be incorporated into the virus as it is being assembled.

“That was the big move for us,” Welsher said, “We didn’t need to use a quantum dot, we didn’t need to use an artificial fluorescent bead. As long as the fluorescent protein was somewhere in the virus, we could spot it.” To create their viral video, Welsher’s team enlisted Duke’s Viral Vector Core to insert a yellow fluorescent protein into their lentivirus.

Now that the virus-tracking microscope is up-and-running, the team is busy building a laser scanning microscope that will also be able to map cell surfaces nearby. “So if we know where the particle is, we can also image around it and reconstruct where the particle is going,” Welsher said. “We hope to adapt this to capturing viral infection in real time.”

Robust real-time 3D single-particle tracking using a dynamically moving laser spot,” Shangguo Hou, Xiaoqi Lang and Kevin Welsher. Optics Letters, June 15, 2017. DOI: 10.1364/OL.42.002390

Kara J. Manke, PhDPost by Kara Manke

Cooking Up “Frustrated” Magnets in Search of Superconductivity

Sara Haravifard

A simplified version of Sara Haravifard’s recipe for new superconductors, by the National High Magnetic Field Laboratory

Duke physics professor Sara Haravifard is mixing, cooking, squishing and freezing “frustrated” magnetic crystals in search of the origins of superconductivity.

Superconductivity refers to the ability of electrons to travel endlessly through certain materials, called superconductors, without adding any energy — think of a car that can drive forever with no gas or electricity. And just the way gas-less, charge-less cars would make travel vastly cheaper, superconductivity has the potential to revolutionize electronics and energy industry.

But superconductors are extremely rare, and are usually only superconductive at extremely cold temperatures — too cold for any but a few highly specialized applications. A few “high-temperature” superconductors have been discovered, but scientists are still flummoxed at why and how these superconductors exist.

Haravifard hopes that her magnet experiments will reveal the origins of high-temperature superconductivity so that researchers can design and build new materials with this amazing property. In the process, her team may also discover materials that are useful in quantum computing, or even entirely new states of matter.

Learn more about their journey on this fascinating infographic by The National High Magnetic Field Laboratory.

Infographic describing magnetic crystal research

Infographic courtesy of the National High Magnetic Field Laboratory

Kara J. Manke, PhD

Post by Kara Manke

Students Share Research Journeys at Bass Connections Showcase

From the highlands of north central Peru to high schools in North Carolina, student researchers in Duke’s Bass Connections program are gathering data in all sorts of unique places.

As the school year winds down, they packed into Duke’s Scharf Hall last week to hear one another’s stories.

Students and faculty gathered in Scharf Hall to learn about each other’s research at this year’s Bass Connections showcase. Photo by Jared Lazarus/Duke Photography.

The Bass Connections program brings together interdisciplinary teams of undergraduates, graduate students and professors to tackle big questions in research. This year’s showcase, which featured poster presentations and five “lightning talks,” was the first to include teams spanning all five of the program’s diverse themes: Brain and Society; Information, Society and Culture; Global Health; Education and Human Development; and Energy.

“The students wanted an opportunity to learn from one another about what they had been working on across all the different themes over the course of the year,” said Lori Bennear, associate professor of environmental economics and policy at the Nicholas School, during the opening remarks.

Students seized the chance, eagerly perusing peers’ posters and gathering for standing-room-only viewings of other team’s talks.

The different investigations took students from rural areas of Peru, where teams interviewed local residents to better understand the transmission of deadly diseases like malaria and leishmaniasis, to the North Carolina Museum of Art, where mathematicians and engineers worked side-by-side with artists to restore paintings.

Machine learning algorithms created by the Energy Data Analytics Lab can pick out buildings from a satellite image and estimate their energy consumption. Image courtesy Hoël Wiesner.

Students in the Energy Data Analytics Lab didn’t have to look much farther than their smart phones for the data they needed to better understand energy use.

“Here you can see a satellite image, very similar to one you can find on Google maps,” said Eric Peshkin, a junior mathematics major, as he showed an aerial photo of an urban area featuring buildings and a highway. “The question is how can this be useful to us as researchers?”

With the help of new machine-learning algorithms, images like these could soon give researchers oodles of valuable information about energy consumption, Peshkin said.

“For example, what if we could pick out buildings and estimate their energy usage on a per-building level?” said Hoël Wiesner, a second year master’s student at the Nicholas School. “There is not really a good data set for this out there because utilities that do have this information tend to keep it private for commercial reasons.”

The lab has had success developing algorithms that can estimate the size and location of solar panels from aerial photos. Peshkin and Wiesner described how they are now creating new algorithms that can first identify the size and locations of buildings in satellite imagery, and then estimate their energy usage. These tools could provide a quick and easy way to evaluate the total energy needs in any neighborhood, town or city in the U.S. or around the world.

“It’s not just that we can take one city, say Norfolk, Virginia, and estimate the buildings there. If you give us Reno, Tuscaloosa, Las Vegas, Pheonix — my hometown — you can absolutely get the per-building energy estimations,” Peshkin said. “And what that means is that policy makers will be more informed, NGOs will have the ability to best service their community, and more efficient, more accurate energy policy can be implemented.”

Some students’ research took them to the sidelines of local sports fields. Joost Op’t Eynde, a master’s student in biomedical engineering, described how he and his colleagues on a Brain and Society team are working with high school and youth football leagues to sort out what exactly happens to the brain during a high-impact sports game.

While a particularly nasty hit to the head might cause clear symptoms that can be diagnosed as a concussion, the accumulation of lesser impacts over the course of a game or season may also affect the brain. Eynde and his team are developing a set of tools to monitor both these impacts and their effects.

A standing-room only crowd listened to a team present on their work “Tackling Concussions.” Photo by Jared Lazarus/Duke Photography.

“We talk about inputs and outputs — what happens, and what are the results,” Eynde said. “For the inputs, we want to actually see when somebody gets hit, how they get hit, what kinds of things they experience, and what is going on in the head. And the output is we want to look at a way to assess objectively.”

The tools include surveys to estimate how often a player is impacted, an in-ear accelerometer called the DASHR that measures the intensity of jostles to the head, and tests of players’ performance on eye-tracking tasks.

“Right now we are looking on the scale of a season, maybe two seasons,” Eynde said. “What we would like to do in the future is actually follow some of these students throughout their career and get the full data for four years or however long they are involved in the program, and find out more of the long-term effects of what they experience.”

Kara J. Manke, PhD

Post by Kara Manke

Mental Shortcuts, Not Emotion, May Guide Irrational Decisions

If you participate in a study in my lab, the Huettel Lab at Duke, you may be asked to play an economic game. For example, we may give you $20 in house money and offer you the following choice:

  1. Keep half of the $20 for sure
  2. Flip a coin: heads you keep all $20; tails you lose all $20

In such a scenario, most participants choose 1, preferring a sure win over the gamble.

Now imagine this choice, again starting with $20 in house money:

  1. Lose half of the $20 for sure
  2. Flip a coin: heads you keep all $20; tails you lose all $20

In this scenario, most participants prefer the gamble over a sure loss.

If you were paying close attention, you’ll note that both examples are actually numerically identical – keeping half of $20 is the same as losing half of $20 – but changing whether the sure option is framed as a gain or a loss results in different decisions to play it safe or take a risk. This phenomenon is known as the Framing Effect. The behavior that it elicits is weird, or as psychologists and economists would say, “irrational”, so we think it’s worth investigating!

Brain activity when people make choices consistent with (hot colors) or against (cool colors) the Framing Effect.

Brain activity when people make choices consistent with (hot colors) or against (cool colors) the Framing Effect.

In a study published March 29 in the Journal of Neuroscience, my lab used brain imaging data to test two competing theories for what causes the Framing Effect.

One theory is that framing is caused by emotion, perhaps because the prospect of accepting a guaranteed win feels good while accepting a guaranteed loss feels scary or bad. Another theory is that the Framing Effect results from a decision-making shortcut. It may be that a strategy of accepting sure gains and avoiding sure losses tends to work well, and adopting this blanket strategy saves us from having to spend time and mental effort fully reasoning through every single decision and all of its possibilities.

Using functional magnetic resonance imaging (fMRI), we measured brain activity in 143 participants as they each made over a hundred choices between various gambles and sure gains or sure losses. Then we compared our participants’ choice-related brain activity to brain activity maps drawn from Neurosynth, an analysis tool that combines data from over 8,000 published fMRI studies to generate neural maps representing brain activity associated with different terms, just as “emotions,” “resting,” or “working.”

As a group, when our participants made choices consistent with the Framing Effect, their average brain activity was most similar to the brain maps representing mental disengagement (i.e. “resting” or “default”). When they made choices inconsistent with the Framing Effect, their average brain activity was most similar to the brain maps representing mental engagement (i.e. “working” or task”). These results supported the theory that the Framing Effect results from a lack of mental effort, or using a decision-making shortcut, and that spending more mental effort can counteract the Framing Effect.

Then we tested whether we could use individual participants’ brain activity to predict participants’ choices on each trial. We found that the degree to which each trial’s brain activity resembled the brain maps associated with mental disengagement predicted whether that trial’s choice would be consistent with the Framing Effect. The degree to which each trial’s brain activity resembled brain maps associated with emotion, however, was not predictive of choices.

Our findings support the theory that the biased decision-making seen in the Framing Effect is due to a lack of mental effort rather than due to emotions.

This suggests potential strategies for prompting people to make better decisions. Instead of trying to appeal to people’s emotions – likely a difficult task requiring tailoring to different individuals – we would be better off taking the easier and more generalizable approach of making good decisions quick and easy for everyone to make.

Guest post by Rosa Li

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