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. Author manuscript; available in PMC: 2014 Jun 21.
Published in final edited form as: Phys Chem Chem Phys. 2013 Mar 20;15(23):8916–8928. doi: 10.1039/c3cp00063j

Fig 8.

Fig 8

Relevant conformations of the dimer. Both R2/wt (a) and R2/ΔK280 (b) show the presence of extended, amylogenic conformations (regions A, B and D) as well as compact conformations. These extended conformations are mainly antiparallel in the case of R2/wt(c), whereas a small parallel population is present in the mutant as well(d). Notably, the mutant populates also conformations with the backbone perpendicular to each other (region C). The letters A,B,C,D refer to the same population in different plots. Snapshots for each set of structures are shown as well. The inset of structure D shows the contact between Q276 and N279. All the simulations were performed in solution with the peptides in their natural charge state (z/n=+2/1 for R2/wt and z/n=+1/1 for R2/ΔK280). See Figure S3 for how CCS values have been evaluated.