image: Researchers from Trinity University and Southwest Research Institute will study stable Rieske proteins, seen here in a crystalized form, found in T. thermophilus, a bacterium that thrives in harsh conditions near deep ocean vents. The project aims to better understand stability mechanisms that might one day be applied to human proteins to address disease.
Credit: Trinity University
SAN ANTONIO — December 10, 2025 — Southwest Research Institute (SwRI) and Trinity University will study Thermus thermophilus, a thermal bacterium with highly stable proteins, to advance scientific understanding of stability mechanisms that could pave the way for advanced treatments for diseases such as Alzheimer’s, ALS and cancer. The project is supported by SwRI and Trinity through a new grant program designed to encourage collaborative research.
Thermus thermophilus is extremely heat tolerant and produces thermostable enzymes and proteins. Originally isolated from a thermal vent in a hot spring, it is a model organism for genetic manipulation, structural genomics and systems biology. Composed of amino acids, proteins serve a range of vital functions in all living organisms, including the human body. However, destabilized proteins misfold, losing their normal function or forming toxic substances that lead to cell death.
Dr. Jonathan Bohmann, a staff scientist at SwRI, and Dr. Laura Hunsicker-Wang, a chemistry professor at Trinity University, will explore the structure of Rieske proteins found in T. thermophilus and a variety of plants, animals and bacteria. SwRI and Trinity will study them both in a natural state and after inducing mutations to one of its amino acid strings in the lab.
“For SwRI’s part, we’re working to determine a baseline for how mutations or changes in a protein can degrade stability,” said Bohmann. “Nearly any structural change will affect the stability of a protein, but some mutation sites are more relevant than others. We want to understand those changes and if small molecules could bind to those sites to restore stability.”
The team will use the SwRI-developed Rhodium™ molecular docking software to screen compounds that could prevent or reverse instability by attaching to Rieske proteins at binding sites along its crystal structure. The goal is to better understand how the Rieske proteins of T. thermophilus can maintain stability at various conditions from room temperature up to 179.6 degrees Fahrenheit. Researchers will also work to identify the protein’s role in energy production.
“Rieske proteins are interesting because their structure and function are very similar to other organisms, including structurally similar proteins in the human body. And yet, its sequence of approximately 200 amino acids, is totally different than human sequences,” said Hunsicker-Wang, “We want to understand those similarities and differences to answer basic scientific questions and to identify methods to prevent diseases associated with protein misfolding.”
This project was funded through the Trinity-SwRI Research Collaboration Grant Program, which fosters advancement of medical and biomedical research in San Antonio. Trinity University and SwRI contributed $250,000 toward three unique biomedical research projects in 2025, the inaugural year for the program.
"Trinity University is thrilled to be collaborating with SwRI, and we look forward to exciting results from this collaboration," said Dr. David Ribble, dean of the D. R. Semmes School of Science.
“We are proud to launch this new focused grant program to grow Trinity and SwRI collaborations, provide opportunities for Trinity students and advance medical breakthroughs that may one day improve and even save lives,” said Dr. Joe McDonough, vice president of the Chemistry and Chemical Engineering Division at SwRI.
To learn more, visit https://www.swri.org/markets/biomedical-health/pharmaceutical-development/drug-discovery/structure-based-virtual-screening.