It’s a common sight — ants marching in an orderly line over and around obstacles from their nest to a food source, guided by scent trails left by scouts marking the find. But what happens when those scouts find a comestible motherlode?

A team of Florida State University researchers led by Assistant Professor of Mathematics Bhargav Karamched has discovered that in a foraging ant’s search for food, it will leave pheromone trails connecting its colony to multiple food sources when they’re available, successfully creating the first model that explains the phenomenon of trail formation to multiple food sources.

Karamched, who also serves as faculty in FSU’s Institute of Molecular Biophysics, and music arts administration graduate student Sean Hartman, published “Walk This Way: Modeling Foraging Ant Dynamics in Multiple Food Source Environments” in the Journal of Mathematical Biology in September.

“The power of mathematics is that we can devise models that reproduce experimentally observed data and make concrete predictions about what will happen next,” Karamched said. “In this case, we uncovered something that hasn’t been described well by other models: if an ant has access to multiple food sources from its nest, it will initially make multiple trails to each of the sources.”

Karamched uses modeling, mathematical analysis and computer simulations to understand and solve problems in neuroscience and cell biology. Hartman, who earned dual bachelor’s degrees from FSU’s Department of Mathematics and College of Music in May 2023 and expects to complete his graduate studies this spring, approached Karamched about assisting with a Directed Individual Study (DIS). DIS allows students in FSU’s Honors Program to work one-on-one with faculty mentors in an open-ended, hands-on research experience and would allow Hartman to be more involved with mathematical modeling.

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Florida State University’s Institute of Molecular Biophysics hosted Venkatraman “Venki” Ramakrishnan, a world-renowned structural biologist and Nobel Prize winner in chemistry Jan. 22 for a wide-ranging lecture covering his research on the ribosome, proteins and crystal structures punctuated by his personal story of persistence and passion.

After the lecture “My Adventures in the Ribosome,” Ramakrishnan met with faculty and students and signed copies of his book, “Gene Machine: The Race to Decipher the Secrets of the Ribosome.”

Some of the most important things I’ve learned include not being afraid to ask for help and keeping in mind that everyone has imposter syndrome, and the most important thing to do is to keep doing your own thing.

— Venkatraman “Venki” Ramakrishnan

“My lab studies the structure and function of the ribosome, which is an ancient molecule in all cells ranging from bacteria to humans,” Ramakrishnan said. “Bacterial ribosomes are the target of many useful antibiotics. However, going back in history, there has always been a pattern of antibiotic resistance or resistance of cells to medicine. Understanding the ribosome’s structure reveals how antibiotics bind to them, which allows us to understand antibiotic function and how the ribosome works. It’s a very fundamental, important molecule that has many ramifications across the entire field.”

After earning his doctoral degree in theoretical physics at age 24, Ramakrishnan was inspired by the mysteries of biology and decided to dedicate his learning to the field of molecular biology. While not possessing any biological science background, he was offered a postdoctoral fellowship at Yale University by Thomas Steitz, a biochemist with whom Ramakrishnan would eventually share a Nobel Prize for their work on the ribosome. Ramakrishnan did not accept the offer but capitalized on this newfound passion and earned his degree in biology at the University of California, San Diego, in 1978 before returning to Yale for a postdoctoral position in chemistry.

“There were so many twists and turns in my journey,” Ramakrishnan said. “I’m so glad I kept my options open. Earning the Nobel Prize wasn’t an end goal, but it vindicated my decision to go into biology and give science another shot. Some of the most important things I’ve learned include not being afraid to ask for help and keeping in mind that everyone has imposter syndrome, and the most important thing to do is to keep doing your own thing.”

In addition to being a Nobel Laureate, Ramakrishnan was knighted by Queen Elizabeth II in the 2012 New Year Honours for his contributions to molecular biology in 2012, and he also served as president of the Royal Society, the U.K.’s National Academy of Sciences and the world’s oldest independent scientific academy, from November 2015 until November 2020. In Cambridge, England, he worked as a group leader of the Medical Research Council Laboratory of Molecular Biology, one of the world’s leading biological science research institutes, for more than 20 years.

“For some of my students, this is a full circle moment. They grew up reading about Venki’s journey and being inspired by it,” said Hong Li, director of FSU’s Institute of Molecular Biophysics and professor of chemistry and biochemistry. “His story is one of persistence, of how he achieved the highest honor in science by taking risks in an unfamiliar territory and how he contributed in a way that has provided essential foundational information about one of the most important molecules in our bodily functions. We’re so thankful to have him visit.”

The 2009 Nobel Prize in Chemistry was awarded to Ramakrishnan and biochemists Steitz and Ada Yonath for their work in researching the ribosome, describing its three-dimensional atomic structure and explaining the mechanism of protein production. Understanding how proteins are synthesized by ribosomes, which serve as the protein factories of cells, not only helps in treating diseases but also forms the backbone of molecular biology experimental systems, including forensic DNA analysis, gene therapy and more.

Ramakrishnan is also a member of the U.S. National Academy of Sciences, a foreign member of the Indian National Science Academy, a member of the American Philosophical Society, a member of the German National Academy of Sciences Leopoldina and a member of the European Molecular Biology organization. He has earned many awards and medals worldwide for his interdisciplinary research spanning biology, physics, chemistry and molecular biophysics.

“We are honored to host Venki Ramakrishnan for this campus visit, and what a great experience this is for the FSU and Tallahassee communities,” said College of Arts and Sciences Dean Sam Huckaba. “He provides a shining example of the power of interdisciplinary research, and his significant contributions display why science research is moving so forcefully in that direction.”

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Florida State University will host a world-renowned structural biologist and winner of the Nobel Prize in Chemistry this month for a series of lectures and a book signing on his interdisciplinary research in biology, physics, chemistry and molecular biophysics.

Nobel Laureate Venki Ramakrishnan will present the public lecture “My Adventures in the Ribosome” on Monday, Jan. 22 at Opperman Music Hall, followed by a signing of his book “Gene Machine: The Race to Decipher the Secrets of the Ribosome.” The event is free and open to the public, but tickets are required and can be reserved at tickets.fsu.edu.

On Tuesday, Jan. 23, Ramakrishnan will deliver the Robson Distinguished Lecture, “Initiation of translation in eukaryotes,” geared toward faculty, postdoctoral researchers and students in the Department of Chemistry and Biochemistry, Institute of Molecular Biophysics, and Department of Biological Science, at the Kroto Auditorium. Registration is not required for the Robson Lecture, but seating is limited.

“Venki Ramakrishnan embodies the spirit of scientific exploration, venturing into challenging problems with a fearless interdisciplinary approach,” said Hong Li, director of the Institute of Molecular Biophysics and professor of chemistry and biochemistry. “Originally trained as a physicist, he was captivated by the mysteries of biology, leading him to switch fields and make groundbreaking discoveries. This captures the essence of the Robson Lecture, sponsored by the Institute of Molecular Biophysics, celebrating scientific pioneers who push boundaries and defy conventional thinking. His remarkable scientific journey is an inspiration to anyone with a curious mind.”

Ramakrishnan received the Nobel Prize in Chemistry for his work on ribosomal structure in 2009, alongside biochemists Thomas A. Steitz and Ada Yonath, and was knighted in 2012 for his contributions to molecular biology. He also served as president of the Royal Society, the United Kingdom’s national academy of sciences and the world’s oldest independent scientific academy from November 2015 until November 2020, and he was a group leader of the Medical Research Council Laboratory of Molecular Biology in Cambridge, England, one of the world’s leading biological science research institutes, for more than 20 years.

The 2009 Nobel Prize in Chemistry was awarded to Ramakrishnan, Steitz and Yonath for researching the ribosome, describing its three-dimensional structure and explaining the mechanism of protein production.

Proteins are often thought of as the macromolecules that provide structure to the human cell, but they also do much more. Few macromolecules are as important as proteins in executing, maintaining and regulating pathways, systems and processes that enable life as we know it. Understanding how proteins are synthesized by ribosomes, the protein factory of the cell, not only helps in treating diseases but also forms the backbone of molecular biology experimental systems, including forensic DNA analysis, gene therapy and more.

Ramakrishnan and his colleagues are confident that this research and the subsequent studies on medical applications for binding ribosomes to various antibiotics can address a large challenge in medicine and help develop a new generation of antibiotics that more specifically inhibit the protein synthesis of bacteria ribosomes. This helps scientists combat antibiotic resistance in bacteria, allowing medicines to better serve their purpose in the human body.

The Robson Distinguished Lecture was established through a generous gift from FSU physics alumnus Brant Watson, a Professor Emeritus of Neurology and Biomedical Engineering at the University of Miami Miller School of Medicine, in honor of his mentor and major professor, FSU Professor Emeritus of Physics Donald Robson.

For more information about the lectures, visit fla.st/3AIHE2AI.

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The gene-editing technology known as CRISPR has led to revolutionary changes in agriculture, health research and more.

In research published in Nature Catalysis, scientists at Florida State University produced the first high-resolution, time-lapsed images showing magnesium ions interacting with the CRISPR-Cas9 enzyme while it cut strands of DNA, providing clear evidence that magnesium plays a role in both chemical bond breakage and near-simultaneous DNA cutting.

“If you are cutting genes, you don’t want to have only one strand of DNA broken, because the cell can repair it easily without editing. You want both strands to be broken,” said Hong Li, professor in the Department of Chemistry and Biochemistry and director of the Institute of Molecular Biophysics. “You need two cuts firing close together. Magnesium plays a role in that, and we saw exactly how that works.”

CRISPR-Cas9 is the most widely used tool for genetic manipulation. The technology uses a repurposed enzyme to bind to DNA, allowing alterations at specified locations in a genome.

Scientists have known that magnesium plays a role in this process, but it was unclear exactly how, and no one had been able to capture time-lapsed images of the process up close. By leveraging a slower version of CRISPR-Cas9, this research showed that magnesium ions in the center of the catalysis reaction hold a key to the near-simultaneous cutting.

“I think a lot of times in science, even though you can infer something, you would like the proof,” Li said. “For instance, with magnesium everybody knows you need it, but not seeing it in action, that’s not complete science, right? You don’t have the same level of understanding of how it functions.”

The researchers used the cryo-electron microscope at FSU’s Biological Science Imaging Resource, which can produce images with near-atomic resolution, to observe metal ions and other atoms at work within the CRISPR-Cas9 enzyme. That allowed them to collect data that not only confirmed their earlier hypotheses but also led to the surprising discovery about how magnesium coordinates double-stranded breaks.

CRISPR made its debut in gene editing in 2013, and since then, scientists have worked to increase its dependability and expand its applicability to a variety of diverse organisms and cell types.

“By altering the active sites — the sets of ‘scissors’ that cut target and non-target DNA strands — we can sway the ability of Cas9 to use alternative metals for cutting,” said doctoral candidate and paper co-author Mitchell Roth. “There’s still a lot to explore with CRISPR.”

Understanding how each element affects the enzyme’s functioning gives scientists insight into what avenues for research might yield new knowledge and uses. Li and her team are planning further research to investigate how CRISPR-Cas9 can be retooled for other purposes.

Co-authors on this paper were former postdoctoral researchers Anuska Das and Jay Rai, doctoral candidate Yuerong Shu, undergraduate student Megan L. Medina and former undergraduate student Mackenzie R. Barakat, all of FSU.

This research was supported by the National Institutes of Health.

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Four Florida State University faculty members are recipients of a new grant from the National Science Foundation that will fund collaborative research aimed at improving our knowledge of an understudied area of biology: the sense of taste.

Distinguished Research Professor of Mathematics Richard Bertram, who also holds appointments in FSU’s Institute for Molecular Biophysics and Program in Neuroscience, will lead the project, funded by a $430,000 grant, to uncover new patterns in the neural codes that communicate our sense of taste using unique mathematical methods.

In “New Approaches for Interpreting Neural Responses to Behaviorally-Relevant Sensory Stimuli,” Bertram, along with Associate Professor Martin Bauer and Assistant Professor Tom Needham in the Department of Mathematics and Assistant Professor Roberto Vincis in the Department of Biological Science and Program in Neuroscience at FSU, will leverage recently developed tools from mathematics and network science to uncover patterns of electrical activity of neurons in the brain that code information about the foods we eat.

“The brain is made up of billions of tiny cells called neurons,” Vincis said. “These neurons communicate through electrical signals to share and process information about the world around us, enabling us to navigate our environment, to shape our behaviors, and to create lasting memories. What we’re trying to understand is the patterns of these electrical signals (i.e., the neural code) that explain sweet and sour, cold and hot, good and bad flavors in the brain, and finally drive our eating choices.”

“We’re applying new math tools that can extract these patterns not typically showcased by traditional methods,” Needham continued.

Using newly developed mathematical techniques, researchers hope to better understand how the brain senses taste, and these techniques can be used in many other areas of neuroscience where large data sets on human brain functions often manifest.

The cross-disciplinary project was born out of experimental data collected by FSU neuroscience doctoral student Cecilia Bouaichi and analyzed by FSU statistics alumnus Camden Neese (M.S., 2022), under the direction of the interdisciplinary team of professors, which resulted in a study published in 2022 in the Journal of Neuroscience. FSU biomathematics doctoral student Audrey Nash has since joined the team and is analyzing new data sets in different ways.

“This project has blossomed into a larger opportunity for biologists like myself to collaborate with mathematicians such as Bertram, Needham and Bauer to leverage new data analysis that will significantly enhance our ability to decipher and extract meaningful insights from large neuroscience data sets,” Vincis said.

As one of NSF’s recently established funding programs, Emerging Mathematics in Biology is intended to facilitate developments of biology-inspired mathematical theories, methodologies and innovative modeling approaches to advance understanding of challenging biological problems. Funding from this program will allow these four FSU scientists to bring on more research assistants to work on the project.

“We’re truly grateful for this NSF funding because it allows the incredible students who work with us daily to continue pursuing their interests in the project,” Bauer said. “Not only does this grant open opportunities for our students to pursue advanced research and travel to conferences, but it makes them more competitive for the impending job market in academia or industry upon their graduation.”

Because this project prompts potential discoveries in both math and biology, scientists have utilized cross-departmental and cross-disciplinary relationships, allowing them to learn from each other weekly and brainstorm new directions for the project according to their respective fields.

For Needham and Bauer, this means using pure math concepts for more concrete applications. For Vincis and Bertram, this means further pursuing the inner workings of the human nervous system from an interdisciplinary perspective. Together, the team plans to build a comprehensive mathematical toolkit for future scientists to apply to brain research on the sense of taste and other concepts.

“I have worked with experimentalists my whole career in both biology and math, and it’s the best part of my job,” Bertram said. “I’m always applying my math towards biological things, so it’s been hugely beneficial having people with many different skillsets on the team. My hope is that through NSF’s support and many others willing to do the work, we can continue to cultivate an environment of interdisciplinary at FSU for professors and students now and in the future.”

To learn more about mathematics research at FSU, visit math.fsu.edu. To learn more about FSU’s biological science and neuroscience research, visit bio.fsu.edu and neuro.fsu.edu.

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