Figure 1
![Figure 1](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2F1471-2202-9-17/MediaObjects/12868_2007_Article_700_Fig1_HTML.jpg)
APP-TM peptides adopt α-helical dimeric structure in SDS micelles. A. Circular dichroism (CD) spectroscopy of APP-TM peptides in the presence of 20 mM SDS at pH 7. The CD spectra of wild-type (●), V717G (○), V717F (□) and T714I (▲) show that all APP-TM peptides form similar highly helical structures in 20 mM SDS. B. Oligomeric state of APP-TM peptides at different concentrations as determined by SDS-PAGE. Wild-type APP-TM peptides were predominantly dimeric under all concentrations tested, while V717G APP-TM peptides formed monomer-dimer mixtures across the same concentration range.