Unraveling the mechanistic roles of protein conformational transitions and water dynamics in ligand binding

NSF Award Search · 01002526DB NSF RESEARCH & RELATED ACTIVIT · $540,000 · view on nsf.gov ↗

Abstract

With the support of the Chemistry of Life Processes Program in the Chemistry Division, Dr. Ao Ma from the University of Illinois Chicago is studying how proteins bind small molecules, a process both common and critical in biology and medicine. In this process of ligand binding, the conformation of proteins changes. This project aims to understand how the conformational changes are coupled to ligand movement and how the changes are also affected by water molecules. The research will use novel computational methods to reveal the step-by-step pathways and driving forces behind ligand binding. The work will help advance the understanding of enzyme function and inform the design of more effective drugs. The project will also enhance education and training through graduate curriculum development, participation in an undergraduate research program, and mentorship of high school students. The proposed research will apply the energy flow theory and generalized work functional method to compute true reaction coordinates and directly simulate the unbiased, natural dynamics of ligand binding. This approach will enable a rigorous dissection of the molecular mechanism of binding. The project will focus on two model systems: HIV-1 protease and PDZ domains, which represent the two prevalent binding paradigms-conformational selection and induced fit. Key factors that determine binding free energies and rate constants will be identified. Information will be generated on how protein conforma

Key facts

NSF award ID
2530676
Awardee
University of Illinois at Chicago (IL)
SAM.gov UEI
W8XEAJDKMXH3
PI
Ao Ma
Primary program
01002526DB NSF RESEARCH & RELATED ACTIVIT
All programs
Estimated total
$540,000
Funds obligated
$540,000
Transaction type
Standard Grant
Period
09/01/2025 → 08/31/2028