After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.

• 1. Extraction of Amyloids from Neurodegenerative Disease Tissues for Structural Analysis2. Cryo-EM Structure Determination of Amyloid Fibrils: Methodology, Insights, and Practical Tools3. Methods for studying molecular architecture of Ab aggregates in tissues using cryo-ET4. Cryo-EM methods to study binding between amyloid fibrils and chemical compounds or ligan5. Dynamics studies of side-chains and hydration shells in amyloid-beta fibrils using deuterium and oxygen-17 solid-state NMR6. Technical aspects of pressure jump NMR applied to the study of Abeta and protein oligomerization7. Characterizations of the beta-amyloid-membrane interaction intermediates8. Time-resolved solid-state NMR studies of oligomer formation.9. Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy10. Single-molecule fluorescence spectroscopy and imaging on heterogeneous amyloid beta aggregation11. Two-dimensional FT-IR methods on amyloid aggregation and folding pathways12. Application of EPR spectroscopy in the structural studies of Aβ oligomers and fibrils13. Identification of amyloid polymorphisms in brain tissues based on conformational-sensitive dyes14. Molecular simulation methods for amyloid-membrane interactions15. How to prepare Alzheimer's amyloid-beta oligomer samples with sufficient quantity and quality for solid-state NMR measurements

After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.

• 1. Extraction of Amyloids from Neurodegenerative Disease Tissues for Structural Analysis2. Cryo-EM Structure Determination of Amyloid Fibrils: Methodology, Insights, and Practical Tools3. Methods for studying molecular architecture of Ab aggregates in tissues using cryo-ET4. Cryo-EM methods to study binding between amyloid fibrils and chemical compounds or ligan5. Dynamics studies of side-chains and hydration shells in amyloid-beta fibrils using deuterium and oxygen-17 solid-state NMR6. Technical aspects of pressure jump NMR applied to the study of Abeta and protein oligomerization7. Characterizations of the beta-amyloid-membrane interaction intermediates8. Time-resolved solid-state NMR studies of oligomer formation.9. Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy10. Single-molecule fluorescence spectroscopy and imaging on heterogeneous amyloid beta aggregation11. Two-dimensional FT-IR methods on amyloid aggregation and folding pathways12. Application of EPR spectroscopy in the structural studies of Aβ oligomers and fibrils13. Identification of amyloid polymorphisms in brain tissues based on conformational-sensitive dyes14. Molecular simulation methods for amyloid-membrane interactions15. How to prepare Alzheimer's amyloid-beta oligomer samples with sufficient quantity and quality for solid-state NMR measurements

After completing studies for the A.B., A.M., and Ph.D. degrees in chemistry at Harvard University, David W. Christianson joined the faculty of the University of Pennsylvania, where he is currently the Roy and Diana Vagelos Professor in Chemistry and Chemical Biology. At Penn, Christianson’s research focuses on the structural and chemical biology of the zinc-dependent histone deacetylases as well as enzymes of terpene biosynthesis. His research accomplishments have been recognized by several awards, including the Pfizer Award in Enzyme Chemistry and the Repligen Award in Chemistry of Biological Processes from the American Chemical Society, a Guggenheim Fellowship, and the Elizabeth S. and Richard M. Cashin Fellowship from the Radcliffe Institute for Advanced Study at Harvard University. Christianson is also a dedicated classroom teacher, and his accomplishments in this regard have been recognized by the Lindback Award for Distinguished Teaching at Penn and a Rhodes Trust Inspirational Educator Award from Oxford University. Christianson has also held visiting professorships in the Department of Biochemistry at Cambridge University and the Department of Chemistry and Chemical Biology at Harvard University. Christianson has served with Prof. Anna Pyle as Co-Editor-in-Chief of Methods in Enzymology since 2015.

• 1. Extraction of Amyloids from Neurodegenerative Disease Tissues for Structural Analysis2. Cryo-EM Structure Determination of Amyloid Fibrils: Methodology, Insights, and Practical Tools3. Methods for studying molecular architecture of Ab aggregates in tissues using cryo-ET4. Cryo-EM methods to study binding between amyloid fibrils and chemical compounds or ligan5. Dynamics studies of side-chains and hydration shells in amyloid-beta fibrils using deuterium and oxygen-17 solid-state NMR6. Technical aspects of pressure jump NMR applied to the study of Abeta and protein oligomerization7. Characterizations of the beta-amyloid-membrane interaction intermediates8. Time-resolved solid-state NMR studies of oligomer formation.9. Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy10. Single-molecule fluorescence spectroscopy and imaging on heterogeneous amyloid beta aggregation11. Two-dimensional FT-IR methods on amyloid aggregation and folding pathways12. Application of EPR spectroscopy in the structural studies of Aβ oligomers and fibrils13. Identification of amyloid polymorphisms in brain tissues based on conformational-sensitive dyes14. Molecular simulation methods for amyloid-membrane interactions15. How to prepare Alzheimer's amyloid-beta oligomer samples with sufficient quantity and quality for solid-state NMR measurements