The calculated β-sheet content for each glutamine-containing peptide along with the macroscopic physical state of the sample are shown in the phase diagram in Figure . Here we see that the neutral P11-2 (Q,0) and +/-2 charged P11-4 (Q,-2) and P11-8 (Q,+2) form similar β-sheet compositions, ranging from 75-85%. The negatively charged P11-4 (Q,-2) showed the highest β-sheet proportion at 85%, while the positively charged P11-8 (Q,+2) showed the lowest proportion at 75%. The neutral P11-2 (Q,0) was intermediate between these values at 78% β-sheet content. The charged peptides, P11-4 (Q,-2) and P11-8 (Q,+2), both form a self-supporting gel. However, despite the similar β-sheet content, P11-2 (Q,0) is observed to form a free-flowing fluid with visible flocculates present. Therefore, β-sheet assembly of P11 peptides is not a sufficient criterion for formations of a percolating gel structure. We interpret that long-range electrostatic repulsion in the self-assembled filaments is required for a self-supporting gel network to form throughout the sample. Without this repulsive contribution to the system, dense flocculates preferentially form.