Results presented in this book showed that mutating Ile41 and Ala42 to hydrophilic residues increases solubility, while mutating the same residues to hydrophobic residues enhances the aggregation propensity. This result suggests that the enhanced aggregation propensity of Abeta42 relative to Abeta40 results from the hydrophobic nature of Ile41 and Ala42 residues (Chapter 2). Fusions of GFP to Abeta mutants containing 8 12 mutations of hydrophobic residues to other hydrophobic residues produced white phenotypes, suggesting that generic hydrophobicity (rather than specific nonpolar side chains)...
Results presented in this book showed that mutating Ile41 and Ala42 to hydrophilic residues increases solubility, while mutating the same residues to ...