Structural Study of Amyloid-β, Volume 729 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on important topics such as the Extraction of Amyloids from Neurodegenerative Disease Tissues for Structural Analysis, Cryo-EM Structure Determination of Amyloid Fibrils: Methodology, Insights, and Practical Tools, Methods for studying molecular architecture of Ab aggregates in tissues using cryo-ET, Cryo-EM methods to study binding between amyloid fibrils and chemical compounds or ligan, Dynamics studies of side-chains and hydration shells in amyloid-beta fibrils using deuterium and oxygen-17 solid-state NMR, and much more.
Additional chapters cover the Technical aspects of pressure jump NMR applied to the study of Abeta and protein oligomerization, Characterizations of the beta-amyloid-membrane interaction intermediates, Time-resolved solid-state NMR studies of oligomer formation, Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy, Single-molecule fluorescence spectroscopy and imaging on heterogeneous amyloid beta aggregation, Two-dimensional FT-IR methods on amyloid aggregation and folding pathways, and much more.
1. Title of Book - p. i 2. Cover image - p. i 3. Title page - p. ii 4. Table of Contents - p. iii 5. Series Page - p. iii 6. Copyright - p. iv 7. Contributors - p. xv 8. Chapter One: Amyloid extraction from neurodegenerative disease tissues for structural studies - p. 1 9. Chapter Two: Cryo-EM structure determination of amyloid fibrils: Methodology, insights, and practical tools - p. 35 10. Chapter Three: In-tissue structural biology of the brain: A focus on Alzheimer’s disease pathology - p. 69 11. Chapter Four: Cryo-EM methods to study binding between amyloid fibrils and chemical compounds - p. 107 12. Chapter Five: Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR - p. 145 13. Chapter Six: Opportunities and challenges in the use of pressure-jump NMR to study Aβ and protein oligomerization - p. 179 14. Chapter Seven: Characterizations of the β-amyloid (Aβ)-membrane interaction intermediates - p. 231 15. Chapter Eight: Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation - p. 259 16. Chapter Nine: Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy - p. 281 17. Chapter Ten: Single-molecule fluorescence spectroscopy and imaging of heterogeneous amyloid β aggregation - p. 309 18. Chapter Eleven: Two-dimensional FTIR methods on amyloid aggregation and folding pathways - p. 333 19. Chapter Twelve: Application of EPR spectroscopy in the structural studies of Aβ oligomers and fibrils - p. 361 20. Chapter Thirteen: All-atom MD simulations of amyloid–membrane interactions: Setup, execution, and analysis - p. 389 21. Chapter Fourteen: How to prepare Alzheimer’s amyloid-β(1-42) oligomer samples with sufficient quantity and quality for biophysical and solid-state NMR measurements - p. 419
Structural Study of Amyloid-β, Volume 729 in the Methods in Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on important topics such as the Extraction of Amyloids from Neurodegenerative Disease Tissues for Structural Analysis, Cryo-EM Structure Determination of Amyloid Fibrils: Methodology, Insights, and Practical Tools, Methods for studying molecular architecture of Ab aggregates in tissues using cryo-ET, Cryo-EM methods to study binding between amyloid fibrils and chemical compounds or ligan, Dynamics studies of side-chains and hydration shells in amyloid-beta fibrils using deuterium and oxygen-17 solid-state NMR, and much more.
Additional chapters cover the Technical aspects of pressure jump NMR applied to the study of Abeta and protein oligomerization, Characterizations of the beta-amyloid-membrane interaction intermediates, Time-resolved solid-state NMR studies of oligomer formation, Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy, Single-molecule fluorescence spectroscopy and imaging on heterogeneous amyloid beta aggregation, Two-dimensional FT-IR methods on amyloid aggregation and folding pathways, and much more.
1. Title of Book - p. i 2. Cover image - p. i 3. Title page - p. ii 4. Table of Contents - p. iii 5. Series Page - p. iii 6. Copyright - p. iv 7. Contributors - p. xv 8. Chapter One: Amyloid extraction from neurodegenerative disease tissues for structural studies - p. 1 9. Chapter Two: Cryo-EM structure determination of amyloid fibrils: Methodology, insights, and practical tools - p. 35 10. Chapter Three: In-tissue structural biology of the brain: A focus on Alzheimer’s disease pathology - p. 69 11. Chapter Four: Cryo-EM methods to study binding between amyloid fibrils and chemical compounds - p. 107 12. Chapter Five: Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR - p. 145 13. Chapter Six: Opportunities and challenges in the use of pressure-jump NMR to study Aβ and protein oligomerization - p. 179 14. Chapter Seven: Characterizations of the β-amyloid (Aβ)-membrane interaction intermediates - p. 231 15. Chapter Eight: Time-resolved solid-state nuclear magnetic resonance studies of amyloid-β oligomer formation - p. 259 16. Chapter Nine: Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy - p. 281 17. Chapter Ten: Single-molecule fluorescence spectroscopy and imaging of heterogeneous amyloid β aggregation - p. 309 18. Chapter Eleven: Two-dimensional FTIR methods on amyloid aggregation and folding pathways - p. 333 19. Chapter Twelve: Application of EPR spectroscopy in the structural studies of Aβ oligomers and fibrils - p. 361 20. Chapter Thirteen: All-atom MD simulations of amyloid–membrane interactions: Setup, execution, and analysis - p. 389 21. Chapter Fourteen: How to prepare Alzheimer’s amyloid-β(1-42) oligomer samples with sufficient quantity and quality for biophysical and solid-state NMR measurements - p. 419
