Direct, all-atom calculations of the free energy of hydration of aqueous deca-alanine structures --- holistically including backbone and side-chain interactions together --- show that attractive interactions and the thermal expansion of the solvent explain the inverse temperature signatures that have been interpreted traditionally in favor of hydrophobic mechanisms for stabilizing the structure and function of soluble proteins.
@article{arxiv.1812.06913,
title = {Long-Range Interactions Dominate the Inverse-Temperature Dependence of Polypeptide Hydration Free Energies},
author = {Dheeraj S. Tomar and Michael E. Paulaitis and Lawrence R. Pratt and D. Asthagiri},
journal= {arXiv preprint arXiv:1812.06913},
year = {2019}
}