From Globular Proteins to Amyloids
eBook - ePub

From Globular Proteins to Amyloids

  1. 278 pages
  2. English
  3. ePUB (mobile friendly)
  4. Available on iOS & Android
eBook - ePub

From Globular Proteins to Amyloids

About this book

From Globular Proteins to Amyloids proposes a model and mechanism for explaining protein misfolding. Concepts presented are based on a model originally intended to show how proteins attain their native conformations. This model is quantitative in nature and founded upon arguments derived from information theory. It facilitates prediction and simulation of the amyloid fibrillation process, also identifying the progressive changes that occur in native proteins that lead to the emergence of amyloid aggregations.- Introduces basic rules for protein folding, along with the conditions that result in misfolding- Presents research that lies in treating the aqueous environment as a continuum rather than a set of individual water molecules (i.e. the classic representation)- Provides practical applications for helping the prevention of amyloidosis and improving drug design

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Yes, you can access From Globular Proteins to Amyloids by Irena Roterman-Konieczna in PDF and/or ePUB format, as well as other popular books in Medicine & Pharmacology. We have over one million books available in our catalogue for you to explore.

Information

Publisher
Elsevier
Year
2019
Print ISBN
9780081029817
eBook ISBN
9780081029824
Topic
Medicine
Subtopic
Pharmacology

Table of contents

  1. Cover image
  2. Title page
  3. Table of Contents
  4. Copyright
  5. Contributors
  6. Preface
  7. Introduction
  8. Chapter 1. Description of the fuzzy oil drop model
  9. Chapter 2. Folding with active participation of water
  10. Chapter 3. Information encoded in protein structure
  11. Chapter 4. Globular or ribbon-like micelle
  12. Chapter 5. Proteins structured as spherical micelles
  13. Chapter 6. Local discordance
  14. Chapter 6.A. The active site in a single-chain enzyme
  15. Chapter 6.B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface
  16. CHAPTER 6.C. Ligand binding cavity encoded as a local hydrophobicity deficiency
  17. Chapter 7. Solenoid – An amyloid under control
  18. Chapter 8. Composite structures
  19. Chapter 9. Non-amyloid structure of the Aβ(1–42) polypeptide in presence of a permanent chaperone
  20. Chapter 9.A. Complexes Aβ(1–42) polypeptide with non-protein molecules
  21. Chapter 9.B. Structure of selected fragments of Aβ(1–42) in complex with other proteins
  22. Chapter 10. Amyloids identification based on fuzzy oil drop model
  23. Chapter 10.A. Amyloid as a ribbon-like micelle
  24. Chapter 10.B. Analysis of alternative conformations of the Aβ(1–40) amyloid protein
  25. Chapter 10.C. Specificity of amino acid sequence and its role in secondary and supersecondary structure generation
  26. Chapter 11. Anti-amyloid drug design
  27. Chapter 12. The hypothetical amyloid transformation of transthyretin
  28. Summary: Protein is an intelligent micelle
  29. Index