The mechanisms by which proteins fold and unfold in aqueous solutions is still not well understood. Depsite urea being a common protein denaturant, there is no atomic level understanding of how this molecule interacts with the functional groups on a protein or peptide in aqueous solution in order to cause unfolding. Here we proposed to measure the beta-turn forming pentapeptide -Tyr-Pro-Gly-Asp-Val-NH2 in water and in aqueous urea solutions in order to understand the details of how the folded peptide is hydrated and how this hydration is or isn't disrupted upon the addition of urea which will unfold the peptide in solution.