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
Professor Irena Roterman-Konieczna her 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. She is the Chief Editor of the journal Bio-Algorithms and Med-Systems (de Gruyter).