Daniel Keedy
Associate Professor
Areas of Expertise/Research
- Structural Biology
- Protein Flexibility
- Phosphatases
Building
CUNY Advanced Science Research Center (ASRC)
Office
3.316
Phone
212-413-3246
Website
Daniel Keedy
Profile
Professor Keedy begin his appointment at CUNY as an Assistant Professor in January 2018 and was promoted to Associate Professor in September 2025. He is affiliated with the Structural Biology Initiative at the CUNY Advanced Science Research Center (ASRC); the Department of Chemistry and Biochemistry at t九色视频 (CCNY); and the Ph.D. Programs in Biochemistry, Biology, and Chemistry at the CUNY Graduate Center. Prior to his appointment at CUNY, Professor Keedy was an A.P. Giannini Postdoctoral Fellow in Bioengineering and Therapeutic Sciences at the University of California, San Francisco working with Professor James Fraser. He earned his Ph.D. in Biochemistry and Structural Biology & Biophysics from Duke University, after receiving his B.A. in Biochemistry & Molecular Biology from Rhodes College. His research on protein structural flexibility, temperature-dependent X-ray crystallography, and allosteric regulation has been supported by funding from the National National Institutes of Health, including the National Institute of General Medical Sciences and the National Institute on Aging, and from the Department of Energy. Professor Keedy has also received a Cottrell Scholar Award and a CCNY CCAPP STEM Teacher of the Year Award.
Education
A.P. Giannini Postdoctoral Fellow, University of California, San Francisco, 2012-2017
Ph.D., Duke University, 2006-2012
B.A., Rhodes College, 2002-2006
Research Interests
Professor Keedy develops experimental and computational methods to control proteins by biasing toward specific conformations that underlie functions such as allostery, ligand binding, and catalysis. His work reveals new opportunities to modulate the activities of therapeutic targets such as tyrosine phosphatases with small molecules and protein engineering, and also offers insights into more general evolutionary processes that led to functional diversity in the human proteome.