This implies that ATP has a capacity in shifting the equilibrium of different conformations, as we recently observed that ATP could enhance the stability without detectable binding by NMR on the ALS-causing C71G mutant of profilin-1 most likely by dynamically interacting with the exposed hydrophobic patches or/and even mediating the hydration shell of proteins28. Here, PFN1 is linked to amyotrophic lateral sclerosis.