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.
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.
Professor Irena Roterman-Konieczna completed her PhD at the Nicolaus Copernicus Medical Academy Krakow, Poland and undertook her postdoctoral studies at Cornell University, USA. She is the director of the Department of Bioinformatics and Telemedicine at Jagiellonian University - Medical College, Poland. Her fields of interest are protein structure, folding simulation as well as systems biology. She is the author of "Protein Folding in Silico", published by Woodhead Publishing in 2012., and "From Globular Proteins to Amyloids" published by Elsevier in 2020. She is the Chief Editor of the journal Bio-Algorithms and Med-Systems (de Gruyter).
Inhaltsangabe
1. Description of the fuzzy oil drop model 2. Folding with the active participation of water 3. Information coded in protein structure 4. Gobular or ribbon-like micelle 5. Proteins structured as spherical micelles 6. Local discordance 6. A. The active site in a single-chain enzyme identified as local deficiency of hydrophobicity 6. B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface 6. C. Ligand binding cavity coded in form of local deficiency of hydrophobicity 7. Solenoid - amyloid under control 8. Composite structures 9. Permanent chaperons 9. A. Non-amyloid structure of the aß(1-42) polypeptide requiring a permanent chaperone 9. B. Structural properties of aß(1-42) chain fragments in complex with proteins acting as permanent chaperones 10. Amyloids 10. A. Amyloid as a ribbon-like micelle 10. B. Alternative conformations of the aß(1-40) amyloid protein 10. C. Specificity of amino acid sequence and its role in secondary and super secondary structure generation 11. Anti-amyloid drug design 12. Predicted structure of the transthyretin amyloid
1. Description of the fuzzy oil drop model 2. Folding with the active participation of water 3. Information coded in protein structure 4. Gobular or ribbon-like micelle 5. Proteins structured as spherical micelles 6. Local discordance 6. A. The active site in a single-chain enzyme identified as local deficiency of hydrophobicity 6. B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface 6. C. Ligand binding cavity coded in form of local deficiency of hydrophobicity 7. Solenoid - amyloid under control 8. Composite structures 9. Permanent chaperons 9. A. Non-amyloid structure of the aß(1-42) polypeptide requiring a permanent chaperone 9. B. Structural properties of aß(1-42) chain fragments in complex with proteins acting as permanent chaperones 10. Amyloids 10. A. Amyloid as a ribbon-like micelle 10. B. Alternative conformations of the aß(1-40) amyloid protein 10. C. Specificity of amino acid sequence and its role in secondary and super secondary structure generation 11. Anti-amyloid drug design 12. Predicted structure of the transthyretin amyloid
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