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. Author manuscript; available in PMC: 2019 Apr 26.
Published in final edited form as: Nat Phys. 2016 Jul 18;12(9):874–880. doi: 10.1038/nphys3828

Fig. 5. The apparent reaction order is controlled by the surface saturation.

Fig. 5

Simulation results: (a) Scaling exponent for the kinetics of fibril self-replication, averaged over the range of concentrations (20μM ≤ c ≤ 1mM), as a function of the interpeptide interaction between soluble monomers at constant peptide-fibril affinity ϵsf = 8kT, and (b) as a function of the peptide-fibril affinity at constant inter-peptide affinity ϵss = 4kT. An increase in ϵss and ϵsf increases the surface coverage, as shown by the representative snapshots in insets, taken at a monomer concentration c = 0.15mM. Experimental results: (c) The average scaling exponent for self-replication of 42 fibrils at a range of NaCl concentrations, whose increase is expected to increase both ϵss and ϵsf from Ref. [18].