Alzheimer's disease is presumed to be caused by the formation of intracellular plaques of amyloid beta (A beta) peptides inside neurons. The most abundant A beta forms are A beta 40 and A beta 42 comprising, respectively, 40 and 42 residues. Recent experiments showed that the triple Gly33Val-Val36Pro-Gly38Val (VPV) mutation causes A beta 42 to become "super-A beta 42" with elevated aggregation rates and toxicity. Upon VPV mutation, oligomerization pathways of A beta 40 become similar to those of the A beta 42 wild type. It was hypothesized that the super behavior of A beta 42 occurs due to an enhanced content of the beta-turn and beta-hairpin, centered at residues 36-37, and the similarity in oligomerization pathways of A beta 40-VPV and A beta 42-WT comes from the increased beta-turn population. As this is based on simulation of the truncated fragments, this hypothesis may not be valid for the full-length case, motivating us to perform all-atom molecular dynamics simulations for full-length A beta sequences. We showed that the results obtained for truncated peptides fall short in explaining the similarity of self-assembly pathways of A beta 40-VPV and A beta 42-WT. Instead, we propose that the similarity is due to not only increased beta-turn population but also due to the elevated beta-structure of the entire sequence. Similar to VPV, the Gly33Val-Val36Asn-Gly38Leu mutation enhances the beta-structure and the C-terminal turn making the behavior of A beta 40 similar to that of A beta 342 -WT.