Understanding how enzyme shapes and movements control their activity
Official title: Exploiting temperature-sensitive orthologs to understand protein allostery
Funded at University of California, Merced · NIH-11361141 · Data updated 2026-11-12
This grant explores how temperature-driven changes in enzyme shapes affect their activity, with the goal of finding hidden states that could help drug discovery.
Quick facts
| Grant type | NIH-funded research |
|---|---|
| Study type | NIH-funded research |
| Funding institution | University of California, Merced NIH-funded |
| Lab location | 1 site (Merced, United States) |
| Project start | August 1, 2023 |
| Project end | June 30, 2028 |
| Funding year | 2026 |
| Award (this year) | $375,957 |
| NIH project number | 5R35GM150936-04 |
| Project ID | NIH-11361141 on NIH RePORTER |
Who could benefit from this research
✓Could help
Not applicable to patient participation in its current form (basic science with enzyme systems); potential future applications may involve patients if targets translate to disease-relevant enzymes.
✕Less likely to help
Direct patient benefits are not part of this basic science grant at this stage.
What this research studies
Researchers will study how the structure, movements, and function of enzymes are connected by using temperature-based methods and advanced X-ray crystallography. They will focus on temperature-sensitive enzyme families like kinases, proteases, and ATP-dependent chaperones to see how different shapes enable or limit activity. The project also aims to reveal cryptic pockets and previously unseen states that could be targeted by drugs, using time-resolved temperature-jump experiments. In addition, the team will keep developing new hardware and software to improve data collection and analysis of enzyme dynamics. Together, these efforts could illuminate how allosteric regulation works at multiple scales inside cells.
Why it matters
Potential benefit: If successful, this work could uncover new drug targets within enzymes by revealing hidden conformations that control activity.
How similar studies have gone: Prior work shows that studying enzyme dynamics can reveal important regulatory states, and this project builds on that foundation with temperature-jump crystallography as a novel approach.
Where this research is happening
-
University of California, Merced
Merced, United States Active
Researchers
- Principal investigator: Thompson, Michael C. — University of California, Merced
- Study coordinator: Thompson, Michael C.
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About this research
- This is an active NIH-funded research project — typically early-stage science, not a clinical trial accepting patient enrollment.
- Some NIH-funded labs run parallel clinical studies or seek volunteers for related work. To check, contact the principal investigator or institution listed above.
- For full project details, budget, and progress reports, visit the official NIH RePORTER page.