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- 278 pages
- English
- ePUB (mobile friendly)
- Only available on web
eBook - ePub
From Globular Proteins to Amyloids
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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
Topic
MedicineSubtopic
PharmacologyTable of contents
- Cover image
- Title page
- Table of Contents
- Copyright
- Contributors
- Preface
- Introduction
- Chapter 1. Description of the fuzzy oil drop model
- Chapter 2. Folding with active participation of water
- Chapter 3. Information encoded in protein structure
- Chapter 4. Globular or ribbon-like micelle
- Chapter 5. Proteins structured as spherical micelles
- Chapter 6. Local discordance
- Chapter 6.A. The active site in a single-chain enzyme
- Chapter 6.B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface
- CHAPTER 6.C. Ligand binding cavity encoded as a local hydrophobicity deficiency
- Chapter 7. Solenoid – An amyloid under control
- Chapter 8. Composite structures
- Chapter 9. Non-amyloid structure of the Aβ(1–42) polypeptide in presence of a permanent chaperone
- Chapter 9.A. Complexes Aβ(1–42) polypeptide with non-protein molecules
- Chapter 9.B. Structure of selected fragments of Aβ(1–42) in complex with other proteins
- Chapter 10. Amyloids identification based on fuzzy oil drop model
- Chapter 10.A. Amyloid as a ribbon-like micelle
- Chapter 10.B. Analysis of alternative conformations of the Aβ(1–40) amyloid protein
- Chapter 10.C. Specificity of amino acid sequence and its role in secondary and supersecondary structure generation
- Chapter 11. Anti-amyloid drug design
- Chapter 12. The hypothetical amyloid transformation of transthyretin
- Summary: Protein is an intelligent micelle
- Index