Biophysics

Molecular Lock and Key: Decoding the Secrets of Ion Binding

Steven Burrows — Wed, 09 Apr 2025 18:25:48 +0000

Molecular Lock and Key: Decoding the Secrets of Ion Binding Steven Burrows Wed, 04/09/2025 - 12:25

Kenna Hughes-Castleberry / JILA Science Communicator

Understanding how molecules interact with ions is a cornerstone of chemistry, with applications from pollution detection and cleanup to drug delivery. In a series of new studies led by JILA Fellow and University of Colorado Boulder chemistry professor Mathias Weber, researchers explored how a specific ion receptor called octamethyl calix[4]pyrrole (omC4P) binds to different anions, such as fluoride or nitrate. These findings, published in The Journal of the American Chemical Society, The Journal of Physical Chemistry Letters, and The Journal of Physical Chemistry B, provide fundamental insights about molecular binding that could help advance fields such as environmental science and synthetic chemistry.

“The main issue with understanding these interactions is that there is a competition between an ion binding to a certain receptor and that same ion wanting to be surrounded by solvent molecules,” Weber explains. “This competition impacts how effective and specific an ion receptor can be, and we currently don’t understand it sufficiently well to design better ion receptors for applications. This has been a problem for decades, and we can now try to solve it by taking a different perspective.”

Looking at Ion Receptors

The test molecule in question, omC4P, is a prototypical anion receptor that has received much interest for nearly 30 years, a macrocyclic molecule with a cup-like structure designed to capture negatively charged ions (anions). Its rigid yet adaptable cavity contains four NH groups that form hydrogen bonds with incoming ions, making it an ideal system for investigating how different anions interact with molecular hosts.

What makes omC4P especially interesting is its specificity. Because its binding pocket has a particular size and shape, simple anions like fluoride or chloride fit quite snugly. However, when larger or more complex anions enter, like nitrate or formate, their shapes can disrupt the pocket structure, and the ions stick out into the surrounding solvent . At the same time, some ions bind strongly to omC4P even though they are relatively large, because they bind tightly to the NH groups.

Understanding these variations in binding is crucial for designing selective receptors. If a receptor can differentiate between closely related anions, it could help significantly in advancing applications such as water purification, medical diagnostics, or industrial sensing.

“These studies help us figure out what makes a receptor highly selective,” elaborates JILA graduate student Lane Terry, the papers’ first author. “If we can fine-tune its structure, we can create targeted ion sensors for real-world applications.”

The many different molecules trying to fill the binding site of octamethyl calix[4]pyrrole (omC4P). Image credit: Steven Burrows / JILA

First Step: Simple Halides

The team’s first study, published in The Journal of the American Chemical Society, focused on halide ions—fluoride, chloride, and bromide—with simple spherical shapes.

“We started with halides because they are the simplest—they act as just a single point charge,” Terry explains.

To analyze how these anions interacted with omC4P, researchers used cryogenic ion vibrational spectroscopy (CIVS) to take a molecular “snapshot” showing the interactions happening in the sample. CIVS is a technique that investigates ionized molecules cooled to low temperatures, which reduces their movement and isolates their vibrations. Ions are then bombarded with infrared photons, causing the ions to absorb specific wavelengths based on how their atoms are arranged and how they vibrate. This, in combination with quantum chemical calculations, allows researchers to measure how the receptor interacts with different ions without interference from external factors like solvent molecules.

After multiple CIVS measurements, the team verified their measurements with those predicted by Density Functional Theory (DFT), a computational method that calculates the molecular structure of complexes to predict how they interact.

“DFT helps us compare our experimental data with theoretical models,” Terry explains, “so we can confirm what we’re seeing and refine our understanding of ion binding.”

Through this process, the team discovered that fluoride formed the strongest hydrogen bonds, remaining tightly bound even in solution, whereas chloride and bromide showed weaker ion-receptor interactions due to weaker proton affinities and thus, more susceptible to solvent interaction.

“This is important because most of these ion receptors are used in aqueous environments,” Terry notes. “Meaning that fluoride’s binding will be more stable with these ion receptors than the other halides.”

Adding Complexity: Nitrate’s Unique Binding

Building on this foundation, the team then explored the nitrate anion binding to omC4P, detailed in The Journal of Physical Chemistry Letters. Unlike halides, nitrate is polyatomic, meaning it has multiple atoms, in this case, arranged in a Y-shape.

Using the CIVS plus DFT method, the researchers found that nitrate prefers a binding mode where only one of its three oxygen atoms interacts with the omC4P’s NH groups. This was a surprising result, as one might expect two oxygen atoms to bind symmetrically.

“Even though nitrate has multiple possible configurations, it strongly favors just one,” Terry says. “The ion shape and charge distribution make a big difference, especially when in an aqueous environment.”

The Most Complex Case: Formate and Isomerism

The final study, published in The Journal of Physical Chemistry B, tackled the most intricate binding behavior yet—formate (HCOO⁻), a small but more asymmetric anion binding to the omC4P. Unlike nitrate, formate was observed to have multiple binding configurations—a process known as isomerism—to the ion receptor.

"Formate actually isomerizes at a low enough energy that we detect multiple isomers, even at cryogenic temperatures,” Terry explains.

The researchers observed that the formate shifted between different configurations, unlike nitrate, which settled into one stable structure. Interestingly, the most stable formate configuration was not symmetrical at all, defying conventional expectations. While highly symmetrical structures often allow for predictable, in contrast, asymmetry can lead to unexpected behaviors that influence selectivity and stability in ion receptors.

After analyzing these findings, the team is now investigating modified omC4P with added structural “walls” to deepen the binding cavity and alter ion interactions, which will add further complexity to their experiment.

Beyond Fundamentals:

While these studies focus on fundamental chemistry, their implications extend far beyond the lab. Environmental monitoring, drug delivery, and chemical sensing all rely on understanding ion interactions at the molecular level.
Terry says, “We work closely with organic chemists who design these molecules. Our findings help them build better ion receptors with improved selectivity.”

Whether detecting contaminants in water or designing better drug carriers, their discoveries bring us one step closer to harnessing chemistry for the greater good.

This research was supported by the National Science Foundation, the JILA Physics Frontier Center, the University of Colorado Boulder, and Colorado State University.

Understanding how molecules interact with ions is a cornerstone of chemistry, with applications from pollution detection and cleanup to drug delivery. In a series of new studies led by JILA Fellow and University of Colorado Boulder chemistry professor Mathias Weber, researchers explored how a specific ion receptor called octamethyl calix[4]pyrrole (omC4P) binds to different anions, such as fluoride or nitrate. These findings provide fundamental insights about molecular binding that could help advance fields such as environmental science and synthetic chemistry.

Off

Traditional

White

Probing Proton Pumping: New Findings on Protein Folding in bacteriorhodopsin (bR)

Steven Burrows — Mon, 05 Feb 2024 18:31:50 +0000

Probing Proton Pumping: New Findings on Protein Folding in bacteriorhodopsin (bR) Steven Burrows Mon, 02/05/2024 - 11:31

Kenna Hughes-Castleberry / JILA Science Communicator

Diagram of the experimental setup (not to scale): Photoactivation of a single molecule of bR. Image Credit: Steven Burrows / JILA

When it comes to drug development, membrane proteins play a crucial role, with about 50% of drugs targeting these molecules. Understanding the function of these membrane proteins, which connect to the membranes of cells, is important for designing the next line of powerful drugs. To do this, scientists study model proteins, such as bacteriorhodopsin (bR), which, when triggered by light, pump protons across the membrane of cells.

While bR has been studied for half a century, physicists have recently developed techniques to observe its folding mechanisms and energetics in the native environment of the cell’s lipid bilayer membrane. In a new study published by Proceedings of the National Academy of Sciences (PNAS), JILA and NIST Fellow Thomas Perkins and his team advanced these methods by combining atomic force microscopy (AFM), a conventional nanoscience measurement tool, with precisely timed light triggers to study the functionality of the protein function in real-time.

“The energetics of membrane proteins hast been challenging to study and therefore not well understood,” explained Perkins. “Using AFM and other methods, we can create ways to look into this further.” Armed with a better understanding of the energetics of these proteins, chemists can design drugs that are more potent towards specific symptoms and illnesses caused by protein misfunction

Measuring Millisecond Protein Dynamics

While bR is a microscopic protein, it can be seen by the naked eye, and even in satellite images, when archaeon microorganisms bloom, they leave vast amounts of it as residue in salt-water ponds. “The ponds become filled with what's called Halobacterium salinarum, the parent organism of bacteriorhodopsin,” Perkins elaborated. “These ponds are used to harvest salt, and because they’re warm and salty, the bacteria love to grow there.”

At the microscopic level, bR works with other membrane proteins to produce energy for the cell by creating a proton gradient on one side of the cell membrane, which ushers the proton through to the other side of the membrane. bR does this by folding and unfolding its helices into specific shapes to control how many protons pass through the membrane. During this process, the proton migration produces chemical energy in the form of adenosine-tri-phosphate (ATP).

For Perkins and his co-author David Jacobson (a former JILA postdoctoral researcher and now an assistant professor at Clemson University), bR presented an opportunity to design a new experimental method for looking at real-time functional energetics. To study proteins like bR, Jacobson, and Perkins utilize AFM, which acts like a tiny finger to pull on the protein gently, which helps the AFM to feel the protein’s surface, mapping out its structure and giving a better understanding of how the protein folds.

Because bR’s folding processes are triggered by light, Perkins and Jacobson added a lighting element to the AFM procedure. “We had this clever idea to glue super thin green LEDs—which trigger the bacteriorhodopsin—to a metal puck, which we can attach to the AFM,” Perkins elaborated. “These green LEDs are also cheap, like $1.00 apiece or $1.50 apiece. Compared to our AFM cantilever, which costs about $80 apiece, throwing away a $1.50 LED is hardly something we worry about.”

With this inexpensive add-on to their AFM, Perkins and Jacobson could induce the bR to fold and unfold with millisecond precision. After collecting their data, the researchers found that the protein correctly folded 60% of the time, allowing the protons to pass through the membrane.
To verify the energetics and real-time function of the protein folding, the scientists mutated the bR protein to remain always in the “open” or unfolded state. Using their new experimental setup, they could reproduce findings similar to what they observed before in the “open” phase of the bR photocycle.

“In biology, you might see something, but you need to ask, am I seeing what I think I'm seeing?” Perkins said. “So, by making a mutation and seeing the effect that we expected, we have increased confidence that we're really studying the process we think we are studying.”

The Mystery of the Misfolded Protein

While Perkins and Jacobson observed proper folding 60% of the time, the other 40% of cases surprised them, as the protein misfolded but could still pump a proton through the membrane. “The misfolding is actually stabilizing,” added Perkins. “And that was really surprising.” In many cases, protein misfolding does not result in stabilization.

Due to the energetic stabilization, Perkins and Jacobson theorized that the bR’s structural helices weren’t separating properly to provide a completely open tunnel for the proton, though it still wiggled through, a process difficult to detect with AFM imaging.

Trying to understand the underlying mechanisms for the misfolding better, Perkins and Jacobson lowered the force on the AFM pulling assay to zero to see if this would coax the protein to fold correctly. However, the results remained the same: 40% of cases resulted in misfolding.
These results, with the same amount of misfolding, puzzled the researchers. While Perkins and Jacobson couldn’t identify the cause of these misfolding cases, they hope to investigate further. Now, they are interested in seeing what the rest of the biophysics community makes of these results.

“There could be more subtle effects, or maybe some new science there,” Perkins added. “It could be that there's a pathway that perhaps people haven't been able to see before.”

Off

Traditional

White

JILA Postdoctoral Researcher Vít Svoboda is Awarded a 2023 JUNIOR STAR project by the Czech Science Foundation

Steven Burrows — Mon, 06 Nov 2023 22:08:50 +0000

JILA Postdoctoral Researcher Vít Svoboda is Awarded a 2023 JUNIOR STAR project by the Czech Science Foundation Steven Burrows Mon, 11/06/2023 - 15:08

Catherine Klauss / JILA Science Communicator

JILA postdoctoral researcher Vit Svoboda

Every year, the Czech Science Foundation (GCAR) funds several JUNIOR STAR projects focused on new research areas and building powerful collaborative teams. These projects are awarded to early-career scientists coming to the Czech Republic from other countries or with significant international experience. Each project is awarded CZK 25 million over the following five years.

This year, JILA postdoctoral researcher Vít Svoboda is one of the 17 awardees in the 2023 JUNIOR STAR cohort. The title of his JUNIOR STAR project: “Probing Chiral Dynamics on Femtosecond Timescales,” will dive into using time-resolved photoelectron spectroscopy to study the physics of chiral molecules during chemical transformations. Congratulations!

Off

Traditional

White

How to Bind with Metals and Water: A New Study on EDTA

Steven Burrows — Thu, 27 Jul 2023 17:30:53 +0000

How to Bind with Metals and Water: A New Study on EDTA Steven Burrows Thu, 07/27/2023 - 11:30

Kenna Hughes-Castleberry / JILA Science Communicator

The near-universal ability of EDTA to accommodate metal cations comes from its molecular flexibility, which allows it to respond to the chemical nature of the metal ion it binds. Image credit: Steven Burrows / JILA

Metal ions can be found in almost every environment, including wastewater, chemical waste and electronic recycling waste. Properly recovering and recycling valuable metals from various sources is crucial for sustainable resource management and contributes to environmental cleanup. Because of the scarcity of some of these metals, such as rare earth elements or nickel, scientists are working to find ways to remove these ions from the waste and recycle the metals. One method used to remove these metals is to bind them to other molecules known as chelators or chelating agents. Chelators have multiple molecular groups that combine to form binding sites with a natural affinity for binding metal ions, making them a natural choice to extract metals from toxic waste. Ethylenediaminetetraacetic acid, or EDTA, is a chelator commonly used in metal removal and many other applications, including medicine. “EDTA is used to treat heavy-metal poisoning,” JILA graduate student Lane Terry explained. “So, if you have lead poisoning, you can take EDTA, which binds to the lead and then safely passes through your system. It's also used as a food preservative. So EDTA is everywhere. It's in one of my topical creams, etc.” EDTA is also commonly used in various laboratories, including many within JILA.

To understand how EDTA binds to these metal ions and water molecules, Madison Foreman, a former JILA graduate student in the Weber group, now a postdoctoral researcher at the University of California, Berkeley, Terry, and their supervisor, JILA Fellow J. Mathias Weber, studied the geometry of the EDTA binding site using a unique method that helped to isolate the molecules and their bound ions, allowing for more in-depth analyses of the binding interactions. They published a series of three papers on this topic. In their first paper, published in the Journal of Physical Chemistry A, they found that the size of the metal ion changes where it sits in the EDTA binding site, which affects other binding interactions, especially with water.

Binding to Metal Ions

EDTA is a chemical commonly found in a chemistry or biology laboratory. “EDTA is employed in many different contexts,” explained Weber. “Whenever you want to get rid of a metal ion in a solution, you throw EDTA into the solution. EDTA will bind to pretty much any metal ion across the periodic table. That's what makes it so widely used in chemistry and biochemistry.” Because of this, EDTA as a model system can reveal more about similar binding behaviors in proteins, including some found in the human body. “People are using it as a model for the binding sites of metal ions in proteins,” said Weber.

However, actually observing the mechanics of EDTA binding is rather tricky. “So, to see exactly what’s going on, you must isolate your target complex from other species,” explained Weber. “That's why we bring these ions into the gas phase, where we can control the number of solvent molecules they interact with, first without any solvent, then selectively start adding solvent one molecule at a time to see what changes.” To do this, the EDTA ions were coaxed into a gas phase. “We then cool them in a cryogenic ion trap to about 50 Kelvin,” Foreman added. “After that, we attach weakly bound nitrogen molecules, which act as messengers telling us later that a photon has been absorbed. We only let those [tagged EDTA] molecules into the second half of the experiment. So there's nothing else, and we have only one sort of ion.”

These tagged ion clusters were then bombarded with light from a tunable laser, which helped detect the target clusters. “We hit that nitrogen-tagged EDTA complex with a photon, which ejects the nitrogen tag,” added Foreman. “So now we have these two fragments flying along, the complex ion and the nitrogen, as well as some amount of undissociated cluster that still has the nitrogen on it.” Thanks to this nitrogen eviction, the researchers can detect that light was absorbed. “After this, we do a second mass spectrometry step to distinguish the undissociated parent ions from the fragment ions,” Weber clarified. “We selectively only measure the intensity of those fragment ions as we tune our laser. That’s how we measure a photo-dissociation spectrum which is the analog of the infrared absorption spectrum of that complex.”

The infrared absorption spectrum of these complexes is something physicists and chemists often refer to, but because multiple atoms and molecules tend to contaminate a sample, this spectrum can be hard to isolate. With their gas-phase method, Weber and his team were able to create an analogous process to the infrared absorption measurements and understand more about the molecular behavior of EDTA. “Now, we can analyze the absorption features from that infrared spectrum to tell us something about the molecular structure,” added Weber. “So encoded in this infrared spectrum is how the EDTA molecule interacts with that metal ion, how its functional groups are oriented, and how that orientation changes as you attach water to it or bring it into solution.”

Binding to Water Molecules

As there is usually water around EDTA and proteins, as in the human body, Weber and his team were curious to understand how EDTA’s behavior changes when interacting with water. “These binding sites in proteins bind to metal ions like calcium or magnesium with similar functional groups as those in EDTA,” Weber explained. “And in proteins, the interaction between the metal ion and the protein binding pocket often does not allow lots of water molecules around it. Instead, it allows one or two in the vicinity. So, one could argue that the behavior of EDTA in the gas phase is actually a good model for trying to understand how these binding sites work.”

In one experiment, published in the Journal of Physical Chemistry Letters, the researchers added water to the metal-EDTA complex one molecule at a time to see how small amounts of water affected the EDTA. “Here you start with just the EDTA metal complex, and then you add one water molecule and see where it binds and how it deforms the metal-EDTA complex as a whole,” Weber added. “Then you can add the second water molecule and see how it influences the complex. In our research, we contrasted it with full solvation, full hydration.”

Studying how EDTA binds metals while in the presence of water can also help researchers better understand the binding processes happening within the human body. “One of the main proteins that EDTA is used to emulate is calmodulin, as its binding pockets are kind of similar,” Foreman explained. “Calmodulin is part of a larger class of proteins. They're all over the body serving all sorts of different functions. But the primary function of calmodulin is as a calcium mediator, so it reacts to the presence of calcium and signals other proteins to perform their functions. This can have effects on everything from hormones to muscle contraction.” Because calmodulin usually binds more to calcium than magnesium in water, the researchers wanted to see if EDTA mimicked this behavior in solution. “When we then look at EDTA, in solution, we see a similar trend in binding affinity, [where EDTA] would prefer to bind calcium than magnesium,” stated Foreman. “So then, by looking at it in the gas phase, or with just a few water molecules, we can see that the structure of the EDTA metal complex does change between magnesium and calcium. And that gives us a hint as to why these proteins might be more selective to some ions than others.”

Recycling Metal Ions

Weber and his team first studied how the molecule binds to alkaline earth metals (such as magnesium, calcium, strontium, or barium) to understand EDTA's interaction with different metal ions. In a second paper, published in 2023 in the Journal of Physical Chemistry A, the researchers found geometric differences in bindings between transition metals, like manganese, cobalt, and nickel, and alkaline earth metals, like calcium or magnesium. “The alkaline earth ions are simple ions. They present a spherically symmetric charge distribution to the outside world,” Weber elaborated. “So they're really round. The transition metals we published in the paper, their electronic structure brings directionality to their bonding with other molecules; they do not look like a spherically symmetric charge distribution. I usually phrase this where the alkaline earth metals are round and the transition metals are spiky. Their electronic structure produces “arms” or “spikes” in a structural template that allows other molecules to bind to them in a very structured way.”

Understanding how EDTA binds to various metals can give Weber and other scientists insight into using molecules that are similar to EDTA in wider applications, such as metal recycling. “Imagine nickel, cobalt, or rare earth metals, everything that you need for things from electric vehicles to batteries to your cell phone,” stated Weber. “These metals need to be removed from electronics waste during recycling; then they need to be purified. One way to do that is to grab them with something [like EDTA] …Lane gathered background information on using chelators for rare earth metal recycling. She actually wrote a proposal on that process. And there are other, very different kinds of ion receptors, too.” They’re hopeful that their results can help other scientists and engineers improve current metal chelation applications.

To understand how EDTA binds to metal ions and water molecules, Madison Foreman, a former JILA graduate student in the Weber group, now a postdoctoral researcher at the University of California, Berkeley, Terry, and their supervisor, JILA Fellow J. Mathias Weber, studied the geometry of the EDTA binding site using a unique method that helped to isolate the molecules and their bound ions, allowing for more in-depth analyses of the binding interactions. They published a series of three papers on this topic. In their first paper, published in the Journal of Physical Chemistry A, they found that the size of the metal ion changes where it sits in the EDTA binding site, which affects other binding interactions, especially with water.

Off

Traditional

White

Looking at a Cellular Switch

Steven Burrows — Tue, 23 May 2023 17:56:28 +0000

Looking at a Cellular Switch Steven Burrows Tue, 05/23/2023 - 11:56

Kenna Hughes-Castleberry / JILA Science Communicator

An artistic rendering of the bacterium's riboswitch and its interactions with three different potential ligands. Image credit: Steven Burrows / JILA

Although one might think it would be simple, the genetics of bacteria can be rather complicated. A bacterium’s genes use a set of regulatory proteins and other molecules to monitor and change genetic expressions within the organism. One such mechanism is the riboswitch, a small piece of RNA that can turn a gene “on” or “off.” In order to “flip” this genetic switch, a riboswitch must bind to a specific ion or molecule, called a ligand, at a special riboswitch site called the aptamer. The ligand either activates the riboswitch (allowing it to regulate gene expression) or inactivates it until the ligand unbinds and leaves the aptamer. Understanding the relationship between ligands and aptamers can have big implications for many fields, including healthcare. “Understanding riboswitches and gene expression can help us develop better antimicrobial drugs,” explained JILA graduate student Andrea Marton Menendez. “The more we know about how to attack bacteria, the better, and if we can just target one small interaction that prevents or abets a gene from being translated or transcribed, we may have an easier way to treat bacterial infections.”

To better understand the dynamics of aptamer and ligand binding, Marton Menendez, along with JILA and NIST Fellow David Nesbitt, looked at the lysine (an amino acid) riboswitch in Bacillus subtilis, a common type of bacterium present in environments ranging from cow stomachs to deep sea hydrothermal vents. With this model organism, the researchers studied how different secondary ligands, like, potassium, cesium, and sodium, affect riboswitch activation, or its physical folding. The results have been published in the Journal of Physical Chemistry B.

Pairing Up Molecules

“We know that cells are complicated; living systems are really complicated,” Marton Menendez stated. “There's a lot going on in them. But when we're trying to study complicated processes, such as how exactly does DNA or RNA fold? we tend to simplify a lot. So, we usually end up reducing the system down to the simplest DNA/RNA structure we want to study and a few necessary salts.” With this idea in mind, Marton Menendez and Nesbitt analyzed their bacterial system using single molecule FRET (fluorescence resonance energy transfer) microscopy. This type of microscopy uses pairs of fluorescent dye molecules to tag specific nucleic acid positions, for this study in particular, a larger RNA riboswitch, allowing researchers to study binding, folding, and unfolding in real time

For this particular riboswitch to work, lysine first binds to the aptamer, which causes the aptamer to fold around lysine. However, in the x-ray crystallography images of the riboswitch, a potassium ion was also bound in the aptamer. According to Marton Menendez: “You can take crystal structures of these pieces of RNA and analyze their content. If the something shows up in the crystal structure, like the potassium ion, it is likely to have been very tightly bound in the riboswitch, because it means that it stayed there a long time. This tells us that potassium can play a ligand-like role for our riboswitch.”

Besides studying potassium as a potential ligand, the researchers also found that when potassium was bound to the riboswitch, it changed how the riboswitch interacted with lysine, the primary ligand. “We looked at how the riboswitch functions with respect to lysine and potassium because they affect each other,” Marton Menendez said, “mainly potassium can tweak some of the lysine’s binding abilities. That's interesting because we think of riboswitches as extremely specific and working only with one specific target molecule.” Instead, in the B. subtilis system, this riboswitch interacts with both lysine and potassium, cooperatively, with the presence of one species enhancing the impact of the other.

A Complex Bacterial Evolution

The idea of RNA regulating its own gene expression suggests that the history of bacterial genetic evolution is more complicated than expected. “If you are an early bacterium, how do you regulate your own genes?” Marton Menendez explained. “"There is a hypothesis that the ancient world had only RNA, no proteins or DNA. So RNA alone was responsible for gene storage and regulation. Riboswitches are an example of how RNA can perform these regulatory functions without protein assistance.” As proteins and more complicated organisms emerged, it is easy to expect these genetic systems to evolve to being more complicated, with a larger number of genes and corresponding regulatory proteins. However, results like Marton Menendez’s and Nesbitt’s suggest that there is more in the bacteria’s genes than meets the eye.

With a more complicated relationship between ligands and aptamers, Marton and Nesbitt were interested to see if this relationship could be found in other bacteria, not just B. subtilis. “There's also a version of a lysine riboswitch that exists in bacteria that live in habitats that are at 80 degrees Celsius, near hydrothermal vents on the sea floor,” elaborated Marton Menendez. “We are preparing a paper comparing how regulation by the lysine riboswitches differs between the two bacteria.”

More Complicated and Cooperative Ligand Relationships

Curious about the flexibility in ligand binding to their aptamer, Marton Menendez and Nesbitt decided to see just how versatile the aptamer could be. “We were also interested to see if potassium ion could then be swapped out for something similar,” Marton Menendez added. “The reason the riboswitch goes for lysine might have something to do with the fact that you've got potassium in the system. But, if you have something that's bigger or smaller than potassium, the riboswitch may have higher or lower binding affinity to lysine.” This experiment suggested an additional project looking at how closely connected the potassium and lysine were as ligands, and also to see if the aptamer would bind to other potential ligand-cation combinations of different sizes. Cations are small positive molecules that organic systems use to regulate different molecular processes.

As Marton Menendez said: “We studied the size effects of ions binding to the riboswitch. The riboswitch typically binds lysine with potassium, so we tested cesium and sodium ions [common molecules within the bacterium] instead of potassium. However, it seems that cesium might be too big and sodium too small to allow lysine to bind properly.” Analyzing the data, the researchers found that the aptamer was quite specific with respect to choice of cation preferentially binding to potassium and lysine as the “perfect Goldilocks combination of sizes.” Most importantly, this finding suggests that riboswitch activity can be regulated with vastly more flexibility by responding cooperatively to more than a single ligand species concentration at a time. This cooperativity is a trick that Nature has long exploited for increasing functionality of proteins (e.g., oxygen bonding to hemoglobin in red blood cells), so it would seem an entirely plausible strategy for nucleic acids as well.

Off

Traditional

White

Life After JILA: Liz Shanblatt

Steven Burrows — Tue, 25 Apr 2023 17:30:18 +0000

Life After JILA: Liz Shanblatt Steven Burrows Tue, 04/25/2023 - 11:30

Kenna Hughes-Castleberry / JILA Science Communicator

Liz Shanblatt, a JILA alumn and a Staff Scientist and Collaboration Manager at Siemens Healthineers

While many JILA alumni go onto have more traditional careers such as in quantum industry, other career paths that might not be as well-known offer some unique benefits. One of these career paths is in medical physics research. Medical physics is an important and rapidly growing field that is dedicated to the application of physics principles and techniques to medicine and healthcare. Medical physicists are experts in the use of radiation and other technologies to diagnose and treat disease, and they play a vital role in ensuring the safety and effectiveness of medical procedures. They also research and develop the next generation of tools for diagnostic imaging and radiation therapy. For JILA alumni Liz Shanblatt, a Staff Scientist and Collaboration Manager at Siemens Healthineers, medical physics became an interest only as she was nearing graduation and starting to look for jobs. “After graduation, I worked as a postdoctoral fellow at the Mayo Clinic Department of Radiology in Rochester, MN,” she explained. “There, I had the opportunity to learn about medical physics and clinical computed tomography (CT) research. CT scanners are constantly under development; the hardware, post-processing, and imaging applications are always being improved. The group I worked with at Mayo had a very close collaboration with Siemens Healthineers, testing and co-developing their latest scanners and algorithms. To support this work, the group has an on-site CT Collaboration Scientist from Siemens.. After finishing my fellowship, I began work with Siemens as one of the on-site CT scientists.”

While Shanblatt didn’t know about medical physics during most of her time at JILA, her work at the institute prepared her well for her future career in this field. “I worked in the Kapteyn/Murnane group on the imaging team,” Shanblatt stated. “My research was on ptychographic coherent diffractive imaging with an ultrafast laser-driven EUV source. This technique involves collecting the far-field diffraction pattern of a sample and computationally reconstructing the amplitude and phase of the object. My projects included developing imaging systems and algorithms for reflection-mode, dynamic, quantitative, and three-dimensional imaging.” Because x-ray-matter interactions, imaging system fundamentals, and image processing are all important aspects of CT physics, Shanblatt found that her work at JILA on these systems translated well to her current position. According to Shanblatt, “I learned a lot of valuable technical skills during my time at JILA, particularly relating to computational imaging, optics, x-ray physics, and imaging system design. More importantly, working at JILA taught me how to think critically and problem solve, and how to effectively work with a team. Any new career will have challenges and new things that need to be learned; scientifically, technically, and interpersonally. Learning how to teach myself new skills and ask for help has been incredible valuable, and working with lots of different people at JILA helped me develop skills to navigate new workplaces and cultures.”

Now as a Staff Scientist and Collaboration Manager at Siemens Healthineers, Shanblatt enjoys being both a researcher and a leader. “My job is essentially a two-in-one: I work as both a scientist and collaboration manager,” she elaborated. “I work closely with an academic research group, supporting the CT research projects with both clinical products and prototypes. I advise on experiments, help troubleshoot hardware and software, and share the team’s feedback with my R&D Colleagues to support product development. I collaborate with radiologists, clinical medical physicists, students, and research fellows to drive CT research and innovate new techniques. I also manage collaboration contracts and keep track of projects and deliverables.” With these many different tasks, Shanblatt enjoys having a balance between an academic focus while working as an industry scientist and seeing those products come to market and make an impact for hospitals and patients.

When thinking back on her time at JILA, Shanblatt is grateful for the many different opportunities the institute presented her. “The research being done at JILA is highly collaborative and produces unique and impactful breakthroughs in many areas of science. JILA also trains well-prepared researchers who go on to work in many different fields of research in both academia and industry. I think that the variety of skills that a JILA researcher has the opportunity to learn helps to make alumni particularly well-suited to take on many different types of careers.” For those who are currently studying at JILA, she offers some key advice: “It’s easy to focus on the most pressing issue in your research project, but make sure to find time to take advantage of all JILA has to offer! Go to the social events and meet new people, network, and learn new skills. Ask others what they are working on, and what’s challenging and exciting about their research. There are also great opportunities to learn machining, electronics, nanofabrication, and many other skills, so take advantage of those resources. Finally, spend time thinking about what truly motivates you and what kind of career and lifestyle you want to have. Find a job that looks interesting, look at what skills they are seeking, and work towards developing those skills.”

Off

Traditional

White

A Look at She Has the Floor

Steven Burrows — Mon, 07 Nov 2022 18:34:38 +0000

A Look at She Has the Floor Steven Burrows Mon, 11/07/2022 - 11:34

Kenna Hughes-Castleberry / JILA Science Communicator

Poster for the "She has the Floor" event

Image Credit: Pretty Brainy

When it comes to inspiring young people to pursue a career within the sciences, you can't start too early. At least, that's what the JILA Excellence in Diversity and Inclusivity (JEDI) group believed when they collaborated with the Colorado non-profit organization Pretty Brainy to develop a speaker series. The series, designed for girls from ages 11 and up, featured the voices of several women JILAns, all focusing on their work and giving tools for success to this younger generation. Over the course of 8 weeks, women of all ages could virtually tune in to hear some of the brightest female minds from JILA discuss the importance of mentorship, perseverance, failure, and of course, some of the newest findings within physics.

In the first event, held on October 5th, JILA Fellow Ann-Marie Madigan spoke on her research within the field of astrophysics, and her day-to-day life as a scientist. "I'll go to work where I'll have a group meeting," Madigan said. "In there, we will discuss our latest results, we might read scientific papers, we might present to each other if we're going to give a talk. It's really good fun. This is a joy in my life, as I'm with really smart people." Madigan elaborated about how fulfilling this job was to her. "It's a really fun job and sometimes it doesn't feel like a job. Sometimes, I'm just walking around, reading, and talking to great people all day."

The next two talks were given by JILA graduate students. Ph.D. student Olivia Krohn, from JILA Fellow Heather Lewandowski's group, discussed her work on molecular collisions in cold, low-pressure environments. “I always knew I liked science and math,” Krohn said. She went on to emphasize the importance of finding what you love to learn about. Similarly, graduate student Rebecca Hirsch of JILA Fellow Mathias Weber's laboratory spoke on her research around cold, gaseous molecules in outer space, giving history on studying space molecules using the Hubble telescope, simulations, and other tools. Both of these talks, given by younger female scientists, inspired many of the young women in the audience, who gave significant positive feedback after each event.

The last two talks of the speaker series were given by JILA staff members: Chief Operating Officer (COO) Beth Kroger, and Science Communicator Kenna Castleberry. Kroger discussed the importance of perseverance for female scientists. “Each of you has already persevered,” Kroger explained. “It helps me to remember that it’s just a bad day, and it won’t always be this way.” In contrast, Castleberry focused on the importance of failing forward. "It's important to use your past mistakes as lessons to learn from, for your future successes," Castleberry explained. "We as female scientists take a lot on, and that can cause us to get overwhelmed and to focus more on our failures. It's important to take a step back and to say no if we have too much going on. No doesn't have to be a scary word."

A bonus talk was later added featuring Dr. Judith Olson from ColdQuanta, a Colorado quantum company.

From the feedback and impact the speaker series had on young women and their families, it was deemed to be a success. No doubt this is just the beginning of a collaboration between JILA JEDI and Pretty Brainy, as both work to inspire powerful young leaders within the scientific community.

Off

Traditional

White

Celebrating 60 Years of JILA

Steven Burrows — Tue, 12 Jul 2022 19:46:03 +0000

Celebrating 60 Years of JILA Steven Burrows Tue, 07/12/2022 - 13:46

Kenna Hughes-Castleberry / JILA Science Communicator

Groundbreaking ceremony for the new JILA laboratory wing and the 10-story office tower, February 25, 1965 (l-r) Lewis Branscomb, Chair of JILA; Donald Hornig, Science Advisor to President Lyndon Johnson; Joseph Smiley, CU President, and Robert Huntoon, Director of the Institute for Basic Standards at NBS. Credit: University of Colorado Publications Service

This year, JILA celebrates its 60th anniversary. Officially established on April 13, 1962, as a joint institution between the University of Colorado Boulder and the National Institute of Standards and Technology (NIST), JILA has become a world leader in physics research. Its rich history includes three Nobel laureates, groundbreaking work in laser development, atomic clocks, underlying dedication to precision measurement, and even competitive sports leagues. The process of creating this science goliath was not always straightforward and took the dedication and hard work of many individuals.

The idea for JILA came from a 1958 meeting of the International Astronomical Union in Moscow. Dr. Lewis Branscombe, a founding member and the head of the atomic physics department of the National Bureau of Standards (NBS, which would later become NIST) proposed an institution for laboratory astrophysics to co-founder, and professor of astrophysics at ��Ҵ�ý�ƽ��, Dr. Richard Thomas. As Branscombe was directly funded by the government, and Thomas by the university, they realized that the best option for such an institution would be a joint establishment between the two entities. Together with the third founding member, Dr. Michael Seaton, a theorist at University College London, they toured nine universities in 1960 and 1961 to find a suitable home for the institution. Finally, the trio settled on ��Ҵ�ý�ƽ�� as the location for their new institution. This was in part due to the President of the university at the time, Quigg Newton, who was supportive of their cause.

In April of 1962, JILA was founded, standing for the Joint Institute of Laboratory Astrophysics. Laboratory astrophysics was of particular interest to the International Astronomical Union as it focused on topics ranging from studying the Sun’s visible light spectrum to developing retroreflecting mirrors.

Aerial view of the newly completed JILA tower situated on the University of Colorado at Boulder campus, 1967. Credit: University of Colorado Publications Service

Trying to find a building on the campus to house JILA, ��Ҵ�ý�ƽ��'s Chief Financial Officer Leo Hill worked with both the NBS and National Science Foundation to pay rent for two floors of the old State Armory building. The NBS also provided funds for laboratory equipment. JILA began construction for its own building shortly after, with the first part, the B-wing, completed in 1966, and the JILA tower finished in 1967. JILA added two more wings to its building, the S-wing (dedicated in 1988), and the X-wing in 2011. There are plans for further expansion with a Y-wing to be built, but nothing is currently in process.

Setting up in the Old Armory building, the JILA scientists (by the early 1960s there were seven scientists at JILA) established several rules that would help JILA function properly. These rules centered around leadership, funding, and fellowships. It was negotiated that with JILA's creation, the NBS would provide instruments and laboratories, while ��Ҵ�ý�ƽ�� would provide researchers and land for the institution. With its unique agreements and roles, JILA’s institute was relatively free to make its own way scientifically. In 1961, ��Ҵ�ý�ƽ��'s Board of Regents approved the title of professor adjoint for any NBS faculty who taught classes at the University. This further solidified the connection between the university and the NBS and made it easier for JILA to attract new scientists.

One of these scientists was Dr. John “Jan” Hall, who was an expert in laser systems and who had previously worked at the NBS location in Washington DC. Though JILA was created during the height of the space race, with the idea being to help the U.S. win this race, Hall helped move JILA in a new direction with laser development. JILA still had ties to astrophysics and astronomy, such as developing lunar lasers for the space race, but the times were changing, and JILA was shifting its research focus to other topics.

Close up of entrance to the old State Armory Building, JILA’s first home on the University of Colorado campus. Credit: JILA

By the late 1960s into the 1970s, JILA's fields were expanding to include laser physics, atomic physics, and others. Hall, at the helm of this shift, helped develop the first high-precision lasers at JILA. His work on these systems would later garner him a Nobel Prize in Physics in 2005.

The 1970s brought a deeper sense of community within JILA, as it was described as a “fun, fast, and free-spirited place.” It was during this time that, along with rafting or ski trips, JILAns also created their own sports leagues, including softball and volleyball. In 1974, JILA elected its first female chair, Katharine Gebbie. Gebbie would later move over to NIST and become their Chief of Quantum Physics Division in 1988, but before she did, she helped recruit and support other female JILA Fellows in JILA. The fields of study within the institution also diversified, as in 1977, the NBS changed the name of their JILA division to the “Quantum Physics Division,” predicting the role that quantum physics would play in JILA'S future.

In the 1980s, JILA was beginning to modernize with the help of the early internet. Thanks to JILA fellow Judah Levine and colleagues the Automated Computer Time Service was brought online, accessible through dial-up modems. This was a monumental first step in modernizing time transfer, as users had access to atomic clock time. By 1988, JILA’s population consisted of more than 200 people, including 23 Fellows. It was also the year that the National Bureau of Standards (NBS)became the National Institute of Standards and Technology (NIST), changing its infrastructure and goals.

More breakthroughs occurred in the 1990s, as JILA once more shifted its mission to reflect NIST's mandate for developing precision measurement, and educating graduate students in future technology. In 1994, JILA had become more than its previous name implied, and dropped the definition of its acronym as the Joint Institute of Laboratory Astrophysics in acknowledgement of the broader scope of science conducted there. In 1995, Nobel-prize winning research was performed by JILA Fellows Carl Weiman and Eric Cornell, as they discovered the Bose-Einstein-Condensate (BEC), a special state of matter helpful for studying quantum dynamics. Nineteen ninety-six brought the 500th Fellows’ meeting, as well as diversity initiatives to make the community more inclusive.

JILA scientists studying in the library on the 10th floor of the JILA tower. Credit: JILA

The 1990s was also an important decade for laser physics at JILA. By 1997, JILA identified seven fields of physics that researchers were studying: atomic physics, chemical physics, materials physics, optical physics, molecular physics, precision measurement, and astrophysics. Laser physics was an underlying study in many of these fields. In 1999, JILA Fellows Margaret Murnane and her husband Henry Kapteyn created what was then the fastest tabletop laser system. That same year, Fellows Jan Hall and Jun Ye developed the first optical frequency comb laser, a tool used by researchers to study optical physics. With these important developments, JILA was quickly establishing a reputation as a world leader in physics research. This reputation boosted JILA's success, as, by the late 1990s, the institution was producing 5–10% of the nation's new Ph.D. graduates in atomic, molecular, and optical (AMO) physics.

The success continued into the 2000s, as the decade brought three Nobel Prizes to JILA. In 2001, Eric Cornell and Carl Weiman were awarded the Nobel Prize in Physics for their work in 1995 on the BEC. The State of Colorado established March 6th as “Carl Weinman and Eric Cornell day” to honor the scientists. A few years later in 2005, Jan Hall also received the Nobel Prize in Physics for his work on laser systems and for developing the first optical frequency comb. JILA also added biophysics as a new field of study, which was helped by the addition of JILA Fellow Thomas Perkins, who worked in this area.

Three JILA Fellows were honored during the 2010s by being selected by then-President Obama to fill important leadership positions within scientific governing groups, including the White House Office of Science and Technology Policy. These Fellows included Carl Weinman, Margaret Murnane, and Carl Lineberger. JILA also celebrated its 50th birthday on April 13th, 2012.

JILA tower (circa 1966) under construction in front of the recently completed laboratory wing, now known as the B-wing of the Duane Physical Laboratories complex. Credit: JILA

Since then, JILA Fellows have received many prestigious scientific awards and grants. The decades of graduate students and postdoctoral researchers who have worked at the institution have gone on to lead successful careers and scientific efforts for other institutions around the world. JILA has also helped spawn many spin-off companies, including 12 companies based in Colorado. These companies range in their products and technology and include companies such as ColdQuanta, Hall Stable Lasers, High Precision Devices, KM Labs, Vescent, to name a few.

With 60 years of scientific research and groundbreaking discoveries, and many successful scientific careers launched, hundreds of lives impacted, it is no surprise that JILA continues to be a global leader in physics research and a pillar within the scientific community. As JILA celebrates its 60th anniversary this year, we look not only to past accomplishments but also to the future, excited to be carrying on such a rich and fulfilling legacy.

Off

Traditional

White

When Breath Becomes Data

Steven Burrows — Tue, 05 Oct 2021 18:26:51 +0000

When Breath Becomes Data Steven Burrows Tue, 10/05/2021 - 12:26

Kenna Hughes-Castleberry / JILA Science Communicator

Model of frequency comb filtering breath molecules. Image credit: Steven Burrows / JILA

There are many ways to diagnose health conditions. One of the most common methods is blood testing. This sort of test can look for hundreds of different kinds of molecules in the body to determine if an individual has any diseases or underlying conditions. Not everyone is a fan of needles, however, which makes blood tests a big deal for some people. Another method of diagnosis is breath analysis. In this process, an individual's breath is measured for different molecules as indicators of certain health conditions. Breath analysis has been fast progressing in recent years and is continuing to gain more and more research interest. It is, however, experimentally challenging due to the extremely low concentrations of molecules present in each breath, limited number of detectable molecular species, and the long data-analysis time required. Now, a JILA-based collaboration between the labs of NIST Fellows Jun Ye and David Nesbitt has resulted in a more robust and precise breath-testing apparatus. In combining a special type of laser with a mirrored cavity, the team of researchers was able to precisely measure four molecules in human breath at unprecedented sensitivity levels, with the promise of measuring many more types of molecules. The team published their findings in the Proceedings of the National Academy of Sciences (PNAS).

Mirrors and Lasers

In order to make an effective breath-testing apparatus, the team of researchers needed a way to "code" the different molecules found in breath into usable data. They did this through a "fingerprinting" process. Using a laser known as a frequency comb, the team could shine over 10,000 different colors of infrared light at the breath sample. According to first author Qizhong Liang, the variation in color was important: "Molecules absorb infrared light in a selective manner. They give different absorption strengths to light at different optical frequencies. How the absorption pattern looks is governed by the molecular rotational and vibrational properties." Since each molecule in the breath absorbed light at a different frequency, this "fingerprinted" each molecule, associating it with a unique absorption pattern, making it easier for the researchers to measure and analyze the data. Liang added that "measuring the optical absorption signals over a broad spectral range, one can simultaneously determine what molecular species are present." As many other devices take tens of minutes, or could only test one molecule species at a time, this new apparatus increased the number of analyzed molecules in breath-testing significantly by analyzing breath in real-time–a reduction in analysis time and presumably, cost.

The implementation of the frequency comb was essential for the apparatus to work. The colors within this special type of laser are evenly spaced in frequency, making them easier to fine-tune than other lasers. In order for the frequency comb to work properly, it has to be coupled to the mirrored cavity by matching the cavity's resonance–a specific frequency that corresponds to the longitudinal mode of that cavity. Depending on the size and shape of the cavity, the resonance may vary. Matching the cavity resonance frequency to the laser frequency helped the team to better measure molecules. "By controlling and matching the light frequency to a specific cavity resonance frequency, one can measure ultrasensitive molecular absorption signals over a broad frequency range in a simultaneous manner," Liang explained. "In our experiment, we can measure absorption signals at 15,000 isolated optical frequencies in just three minutes. This allows us to detect multiple molecular species in a highly time-efficient manner." The increased efficiency made the apparatus capable of measuring and analyzing data in almost real-time.

In building their effective apparatus, the researchers realized that some molecules in breath had very weak light absorption. To boost this absorption, the team built a cavity with a pair of high-reflectivity mirrors. The mirrors enhanced the interaction length between the laser light and breath molecules by a factor of several thousand in order to make the absorption stronger in just one breath. The mirrored cavity increased the sensitivity of the apparatus, furthering its precision.

Testing the Breath: Bananas...and Booze?

After the apparatus was constructed, the researchers needed to test its effectiveness. They decided to look at methanol as a target molecule. In order to see possible changes in methanol levels, they had a test subject consume foods and drinks in an effort to change the methanol levels in their breath. "We actually started with alcohol, because there are some literature reviews in the past that suggest some change in the methanol levels of breath," Liang grinned. "This sounds like a fun experiment because your test subject gets the opportunity to drink alcohol. We tried brandy, whisky and soju, a South Korean wine. It turns out none of these alcohols actually gave some obvious change in molecular concentrations." Though drinking alcohol in the name of science would have been a rather whimsical endeavor, the team ultimately had to abandon the idea.
Instead, they turned to fruit, and found that collecting data in 15-minute intervals, while their test subject ate ripe bananas, resulted in a gradual increase of methanol concentration in the breath. Liang found the entire process to be: "…very impressive. We could monitor several other molecules simultaneously, like methane and partially-deuterated water. We could confirm their concentrations did not change over the time after the banana consumption."

COVID-19 Ready

After seeing success in their apparatus, the team of researchers is shifting their focus towards diagnosing COVID-19 in people. According to postdoctoral researcher Jutta Toscano: "We are currently conducting a campus-wide study to understand how much the molecules present in people's breath can tell us about the state of their health, including the presence of various conditions that could be affecting them, such as COVID-19, diabetes, and asthma, among others." Having a less invasive method to diagnose COVI9-19 will not only make it easier to contain the virus, but can also be a cheaper and faster option for the government in the long run. Toscano found that: "Collaborating and learning from people in other fields of research (from engineering to physiology) has been a very exciting part of this project. Building bridges across disciplines and sharing expertise to reach a common scientific goal is both fulfilling and formative." Such collaborations as this can result in timely and beneficial real-world applications, like the breath-analyzer apparatus, which may change the way COVID-19 infections are analyzed and treated.

Breath analysis has been fast progressing in recent years and is continuing to gain more and more research interest. It is, however, experimentally challenging due to the extremely low concentrations of molecules present in each breath, limited number of detectable molecular species, and the long data-analysis time required. Now, a JILA-based collaboration between the labs of NIST Fellows Jun Ye and David Nesbitt has resulted in a more robust and precise breath-testing apparatus. In combining a special type of laser with a mirrored cavity, the team of researchers was able to precisely measure four molecules in human breath at unprecedented sensitivity levels, with the promise of measuring many more types of molecules.

Off

Traditional

White

JILA Fellows Thomas Perkins and Graeme Smith win the 2021 Outstanding Postdoc Mentor Award

Steven Burrows — Thu, 16 Sep 2021 20:25:09 +0000

JILA Fellows Thomas Perkins and Graeme Smith win the 2021 Outstanding Postdoc Mentor Award Steven Burrows Thu, 09/16/2021 - 14:25

Kenna Hughes-Castleberry / JILA Science Communicator

Photo of JILA Fellows Graeme Smith and Thomas Perkins

JILA Fellow Thomas Perkins has been awarded the 2021 Oustanding Postdoc Mentor Award. This award recognizes mentors who have gone above and beyond to support their postdocs. Perkins was nominated by postdoc David Jacobson, who praised Perkins' effort to help Jacobson apply and receive the prestigious NIH K99 “Pathway to Independence” Award.

JILA Fellow Graeme Smith also won the 2021 Outstanding Postdoc Mentor Award, being nominated by ��Ҵ�ý�ƽ�� postdoc Vikesh Siddhu and former ��Ҵ�ý�ƽ�� postdoc, Felix Leditzky. Leditzky said Smith “played an integral part in guiding me through the process and helping me achieve this career goal. I aim to pay forward the trust and support that I received from him.”

JILA Fellow Thomas Perkins has been awarded the 2021 Outstanding Postdoc Mentor Award. This award recognizes mentors who have gone above and beyond to support their postdocs. Perkins was nominated by postdoc David Jacobson, who praised Perkins' effort to help Jacobson apply and receive the prestigious NIH K99 “Pathway to Independence” Award.

JILA Fellow Graeme Smith also won the 2021 Outstanding Postdoc Mentor Award, being nominated by ��Ҵ�ý�ƽ�� postdoc Vikesh Siddhu and former ��Ҵ�ý�ƽ�� postdoc, Felix Leditzky. Leditzky said Smith “played an integral part in guiding me through the process and helping me achieve this career goal. I aim to pay forward the trust and support that I received from him.”

Off

Traditional

White