Depending on the volume of the simulated system, and the supersaturation of the mother phase, the deviation between a macroscopic and a finite-size nucleation free energy profile can be responsible for significant changes to the outcome of nucleation simulations. In supersaturated solutions, confinement leads to a minimum in the free energy profile shown in Figure A, the depth of which is determined by the initial concentration and number of monomers in solution. Furthermore, the height and position of the barrier is perturbed compared to the macroscopic case. If association of monomers leads to the solution becoming undersaturated below the critical size of the nucleus in the macroscopic limit, then nucleation can be inhibited altogether. One could take advantage of the limitations imposed by finite size by performing simulations initiated with different 𝑁 and 𝑉 and then analysing the steady-state properties of the system obtained from simulations to evaluate Δ𝐹 (𝑛). For example, Li et al. performed a series of unbiased MD simulations where they varied the concentration and total number of coarse-grained, intrinsically disordered peptides in a continuum solvent. Starting from a homogeneous phase, spontaneous separation occurred when simulations were sufficiently large and concentrated, resulting in dense liquid peptide droplets in equilibrium with lean solutions. Fitting the steady-state simulation data to a model analogous to Eq. 7 allowed the authors to evaluate 𝑥 𝑖, * , 𝜎 and 𝑛 * over a range of saturation levels and identify the conditions where nucleation is completely inhibited by the system size .