Figure 4

Apparent dissociation constants of APP-TM peptides in SDS micelles. The apparent dimer dissociation constants for wild-type and mutant APP-TM peptides were determined by examining the concentration dependence of FRET in equimolar mixtures of donor- and acceptor-labeled peptides. The FRET signals were converted to percent dimer and plotted against total APP-TM peptide concentration. The apparent dissociation constants are as follows: 10.3 μM (wild-type), 20.4 μM (V717G), 125 μM (V717F) and 395 μM (T714I).