From Globular Proteins to Amyloids

<p>1. Description of the fuzzy oil drop model<br>2. Folding with the active participation of water<br>3. Information coded in protein structure<br>4. Gobular or ribbon-like micelle<br>5. Proteins structured as spherical micelles<br>6. Local discordance<br>6. A. The active site in a single-chain enzyme identified as local deficiency of hydrophobicity<br>6. B. Protein-protein interaction encoded as an exposure of hydrophobic residues on the surface<br>6. C. Ligand binding cavity coded in form of local deficiency of hydrophobicity<br>7. Solenoid – amyloid under control<br>8. Composite structures<br>9. Permanent chaperons<br>9. A. Non-amyloid structure of the aβ(1-42) polypeptide requiring a permanent chaperone<br>9. B. Structural properties of aβ(1-42) chain fragments in complex with proteins acting as permanent chaperones<br>10. Amyloids<br>10. A. Amyloid as a ribbon-like micelle<br>10. B. Alternative conformations of the aβ(1-40) amyloid protein<br>10. C. Specificity of amino acid sequence and its role in secondary and super secondary structure generation<br>11. Anti-amyloid drug design<br>12. Predicted structure of the transthyretin amyloid</p>