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Robert Tycko, Ph.D., NIH Distinguished Investigator

Robert Tycko.
Scientific Focus Areas: Biomedical Engineering and Biophysics, Chemical Biology, Structural Biology

Professional Experience

  • 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).

Research Goal

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.

Current Research

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.

Select Publications

Experimental Evidence for Millisecond-Timescale Structural Evolution Following the Microsecond-Timescale Folding of a Small Protein.
Wilson CB, Yau WM, Tycko R.
Phys Rev Lett (2024 Jan 26) 132:048402. Abstract/Full Text
Structures of brain-derived 42-residue amyloid-β fibril polymorphs with unusual molecular conformations and intermolecular interactions.
Lee M, Yau WM, Louis JM, Tycko R.
Proc Natl Acad Sci U S A (2023 Mar 14) 120:e2218831120. Abstract/Full Text
View More Publications

Research in Plain Language

We develop new methods for learning the structures of proteins and other molecules that play central roles in human disease. We apply these methods to specific problems where more conventional methods are not adequate. As an example, we developed detailed models of amyloid fibrils that are linked to Alzheimer's disease and type 2 diabetes. Our models reveal the molecular interactions that lead to amyloid formation. This knowledge may inform the design of new chemical compounds to inhibit amyloid formation and for diagnostic imaging.

Last Reviewed April 2024