Supplementary Figure 5: Hydrogen bonding, π/sp2 and hydrophobic interactions calculated from two-chain simulations of FUS120-163.
From: Molecular interactions underlying liquid−liquid phase separation of the FUS low-complexity domain
A) Comparison of the amino acid frequencies found within the low complexity domain of FUS and average disordered and globular proteins24. B) Per-residue hydrogen bonds between each residue of the sequence and different residue types in the other chain. Error bars represent the standard error of the mean for five equal blocks. Tyrosine and glutamine residues are highlighted with gray and red bars respectively. C) Average number of hydrogen bonds formed by each residue of the FUS120-163 sequence in simulation. For the two-chain simulation (dimer) case, only intermolecular hydrogen bonds are considered, and for the single chain simulation (monomer), neighbors of sequence separation of 5 residues or fewer are not counted. D) Average number of hydrophobic contacts formed by each residue of the FUS120-163 sequence in simulation. For the two-chain (dimer) case, only intermolecular hydrogen bonds are considered, and for single chain (monomer), neighbors of sequence separation of 5 residues or fewer are not counted. E) Average number of intermolecular hydrogen bonds, sp2 or hydrophobic contacts between all residues of chain 1 with each residue of chain 2. F). Average total number of hydrogen bonds, sp2 or hydrophobic contacts between residues of type X in chain 1 with type Y in chain 2. Simulation data are plotted as mean ± s.e.m of n=5 equal divisions of the total data.
