Skip to main content
. Author manuscript; available in PMC: 2018 Feb 8.
Published in final edited form as: J Am Chem Soc. 2016 Nov 10;138(46):15197–15203. doi: 10.1021/jacs.6b08665

Figure 5.

Figure 5

Changing the structural preference for 26 length repeats by making point mutations alters the nucleation behavior at 300 K. (A) An inserted L-PG mutation makes the hairpin conformation more favorable. (B) The free energy profile as a function of the number of total residue–residue contacts in a simulation system with six Q12PGQ12 peptide chains. Representative structures in each basin illustrate the progression through the different oligomeric states. (C) The grand canonical free energy for different oligomer states as corrected for the finite size effect for different concentration of free monomers.