From Globular Proteins to Amyloids
- 1st Edition - October 2, 2019
- Latest edition
- Editor: Irena Roterman-Konieczna
- Language: English
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 prote… Read more
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Description
Description
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.
Key features
Key features
- 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
Readership
Readership
Researchers interested in problems related to amyloid formation and protein folding/mis-folding. Students of medicine, pharmacy and pharmacology where protein folding is taught as part of the basic biochemistry curriculum. Pharmaceutical companies which engage in R&D activities related to drug design
Table of contents
Table of contents
Foreword
Irena Roterman
introduction
Konieczny Leszek and Irena Roterman
1. Description of the fuzzy oil drop model
Banach Mateusz, Konieczny Leszek and Irena Roterman
2. Folding with the active participation of water
Gadzała Małgorzata, Dułak Dawid, Banach Mateusz, Konieczny Leszek, Irena Roterman, Stapor Katarzyna and Fabian Piotr
3. Information coded in protein structure
Konieczny Leszek and Irena Roterman
4. Glubular or ribbon-like micelle
Konieczny Leszek and Irena Roterman
5. Proteins structured as spherical micelles
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. Local discordance
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. A. The active site in a single-chain enzyme identified as local deficiency of hydrophobicity
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface
Banach Mateusz, Konieczny Leszek and Irena Roterman
6. C. Ligand binding cavity coded in form of local defficiency of hydrophobicity
Banach Mateusz, Konieczny Leszek and Irena Roterman
7. Solenoid – amyloid under control
Banach Mateusz and Irena Roterman
8. Composite structures
Banach Mateusz, Irena Roterman and Konieczny Leszek
9. Permanent chaperons
Banach Mateusz and Irena Roterman
9. A. Non-amyloid structure of the aβ(1-42) polypeptide requiring a permanent chaperone
Banach Mateusz and Irena Roterman
9. B. Structural properties of aβ(1-42) chain fragments in complex with proteins acting as permanent chaperones
Banach Mateusz and Irena Roterman
10. Amyloids
Banach Mateusz and Irena Roterman
10. A. Amyloid as a ribbon-like micelle
Banach Mateusz and Irena Roterman
10. B. Alternative conformations of the aβ(1-40) amyloid protein
Gadzała Małgorzata, Dułak Dawid, Banach Mateusz and Irena Roterman
10. C. Specificity of amino acid sequence and its role in secondary and supersecondary structure generation
Banach Mateusz and Irena Roterman
11. Anti-amyloid drug design
Banach Mateusz, Konieczny Leszek and Irena Roterman
12. Predicted structure of the transthyretin amyloid
Banach Mateusz, Konieczny Leszek and Irena Roterman
Summary – the protein is an inteligent micelle
Irena Roterman
Product details
Product details
- Edition: 1
- Latest edition
- Published: October 2, 2019
- Language: English
About the editor
About the editor
IR