Robert Tycko, Ph.D.
Laboratory of Chemical Physics
Building NIHBC 05, Room 409
5 Memorial Dr
Bethesda, MD 20892
+1 301 402 8272
The purpose of our research is twofold: (1) to expand the capabilities of experimental techniques, especially solid state NMR techniques, for probing structural properties of molecules with central roles in biology and human disease; (2) to provide new structural and mechanistic information about specific biomolecular systems, including protein assemblies that are associated with Alzheimer’s disease, type 2 diabetes, and AIDS.
My lab is currently pursuing several distinct but inter-related projects. We are using solid state NMR and electron microscopy to characterize molecular structures of amyloid-β fibrils, including fibrils that develop in brain tissue of Alzheimer’s disease patients. We are developing new experimental methods that allow detailed molecular structural studies of transient intermediates in processes such as protein folding, ligand binding, peptide aggregation, and protein self-assembly. We are investigating the structural and physical basis for fibril formation by low-complexity protein sequences. We are using solid state NMR and electron microscopy to characterize protein assemblies that mimic assemblies within HIV-1 and SARS-CoV-2 virions. And we are developing ultra-low-temperature methods for sensitivity enhancement in biomolecular solid state NMR and resolution enhancement in magnetic resonance imaging.
- Senior Investigator, LCP, NIDDK, NIH, 1994-present
- Member of Technical Staff (Principal Investigator), Physical Chemistry Research Department, AT&T Bell Laboratories, 1986-1994
- Postdoctoral Researcher, University of Pennsylvania, 1984-1986
- Ph.D., University of California at Berkeley, 1984
- A.B., Princeton University, 1980
- Fellow of the American Physical Society (1997), the American Association for the Advancement of Science (2005), the International Society of Magnetic Resonance (2008), and the American Academy of Arts and Sciences (2017). Member of the National Academy of Sciences (2020).
Jeon J, Yau WM, Tycko R. Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase. J Am Chem Soc. 2020;142(50):21220-21232.
Ghosh U, Thurber KR, Yau WM, Tycko R. Molecular structure of a prevalent amyloid-β fibril polymorph from Alzheimer's disease brain tissue. Proc Natl Acad Sci U S A. 2021;118(4).
Lee M, Ghosh U, Thurber KR, Kato M, Tycko R. Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS. Nat Commun. 2020;11(1):5735.
Murray DT, Kato M, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R. Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains. Cell. 2017;171(3):615-627.e16.
Chen HY, Tycko R. Low-temperature magnetic resonance imaging with 2.8 μm isotropic resolution. J Magn Reson. 2018;287:47-55.
Related Scientific Focus Areas
Biomedical Engineering and Biophysics
This page was last updated on April 29th, 2022