Learning the Hydrophilic, Hydrophobic and Aromatic Character of Amino Acids from their Interfacial Thermal Conductance in Water

Abstract

In this study, the thermal relaxation of the 20 naturally occurring amino-acids in water is investigated using transient non-equilibrium molecular-dynamics simulations. By modeling the thermal relaxation process, the relaxation times of the amino-acids in water occurs over a timescale covering 2-5 ps. For the hydrophobic amino acids, the relaxation time is controlled by the size of the hydrocarbon side chain, while for hydrophilic amino acids, the number of hydrogen bonds do not significantly affect the timescales of the heat dissipation. Our results show that the interfacial thermal conductance at the amino-acid water interface is in the range of~40-80 MWm$^{-2}$K$^{-1}$. Hydrophobic and aromatic amino acids tend to have a lower interfacial thermal conductance. Notably, we reveal that amino acids can be classified, in terms of their thermal relaxation times and molar masses, into simply connected phases with the same hydrophilicity, hydrophibicity and aromaticity.