Formation of U(SO) is an entropically and thermodynamically favorable reaction. Viscoelastic properties in fluids cause them to snap back to entropically favorable conformations. This is enthalpically unfavorable as solute-solute interactions are breaking but is entropically favorable. Longer stretches of DNA are entropically elastic under tension. Thus in some case greater positional order will be entropically favorable. At higher temperatures, the entropically favored species, the water hydrogen-bonded to the "N"-terminus, was preferred. Thus, any event that would minimize such a surface is entropically favored. Entropically favorable changes in protein dynamics have also been implicated in cAMP mediated EPAC activation.