Adenosine triphosphate (ATP), one of the biologically most important molecules, offers certain anomalous behavior during folding and liquid–liquid phase separation of proteins and RNAs. ATP can act as a “biological hydrotrope”, i.e., it solubilizes hydrophobic proteins or other biomolecules. However, upon exceeding the physiological concentration range (2–10 mM), aggregation of proteins and RNAs is promoted, an effect that is not understood yet. Here we present a time-domain and frequency-domain Terahertz (THz) spectroscopic investigation to understand the solvation of ATP with varying concentration in the range of 2–15 mM. Both time and frequency domain studies of the solvation of adenosine (Adn), sodium triphosphate (TPP), and ATP elucidate that both the adenosine as well as the triphosphate moiety contribute to nearly equal propensity towards the solvation structure of ATP at low concentrations …