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. 2009 Dec 22;7(12):e1000262. doi: 10.1371/journal.pbio.1000262

Figure 4. PXX33 atomic structure derived from solution NMR.

Figure 4

(A) The five lowest energy structures selected from 200 calculated structures represented in ribbon form. While the overall structure was similar between all five conformations, there was a greater variability at the N-terminal PXX12 region. (B) Backbone ribbon representation and side chain heteroatom representation of one PXX33 lowest energy structure. Three polyproline II helix regions—P13–P16 (PPII-1), P19–P22 (PPII-2), and P28–P31 (PPII-3) —are labeled. (C–D) Increase in surface area in larger PXX33 polypeptides (C) versus PXX12 polypeptides (D), resulting in increased interaction, van der Waals attraction, and denser aggregates.