Timothy Street

Timothy Street is an Associate Professor in the Department of Biochemistry at Brandeis University. His research focuses on molecular mechanisms of protein folding and chaperone function, particularly the role of Hsp90 and related chaperones in regulating protein stability and cellular processes. His work integrates structural biology, biophysics, and computational modeling to understand how chaperones influence protein folding and disease-related mechanisms.

Education:

• Ph.D., Johns Hopkins University
• B.S., University of California, Berkeley

Research Interests: Molecular chaperones, protein folding, Hsp90 regulation, cellular protein degradation, insulin-like growth factors, and therapeutic protein design. His lab employs techniques such as X-ray crystallography, NMR, and in-vivo biosensors to study chaperone dynamics and their applications in biomedicine.

Key Contributions:

• Elucidation of Hsp90 conformational changes and their role in substrate binding.
• Discovery of pH-dependent ATPase activity in bacterial Hsp90.
• Development of methods to analyze ribosome profiling and chaperone interactions.

Awards:

• High honors in physics (UC Berkeley, 2001)
• Burroughs-Wellcome Predoctoral Training Fellowship (2004)

Labs/Teams: Affiliated with the Rosenstiel Basic Medical Sciences Research Center, where his lab explores chaperone mechanisms and their biomedical applications.