Direct, all-atom calculations of the free energy of hydration of aqueous deca-alanine structuresholistically 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. Keywords: polypeptide hydration free energies -long-range interactions -inverse temperature dependence I. SIGNIFICANCE STATEMENT [1] Gao A, et al. (2018) Role of solute attractive forces in the atomic-scale theory of hydrophobic effects. J. Phys. Chem. B 122(23):6272-6276. PMID: 29767526.