Abstract
Liquid-liquid phase separation of proteins is a fast growing area of biophysical inquiry due to the role it plays in the formation of membraneless organelles, disease-associated protein aggregation, and disordered protein domains in signaling. Examining these processes in the context of entropy and enthalpy changes is necessary to establish a thermodynamic foundation with which to understand phase transitions. Our previous work probed the phase separation of glycine-rich pentapeptides and found that a loss of conformational entropy upon phase separation is compensated for by a decrease in peptide interaction enthalpy.
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