UV resonance Raman spectroscopy was used to probe the temperature dependence of the conformation of TTR(105-115) in solution. Resonance Raman spectra with excitation at 239.5 nm, show an increase in the absolute resonance Raman cross section of Tyr with an increase in temperature. This trend is associated with an increase in the hydrophobicity of the Tyr local environment, suggesting a conformational change at 28 degrees C. Excitation at similar to 200 nm is known to enhance scattering due to amide vibrations and provides insights as to the secondary structure of a peptide or protein. UVRR spectra at this excitation suggest that in solution the peptide assumes a disordered conformation with frequent formation of beta-turns. Explicit-solvent replica-exchange MD simulations of the isolated peptide in the region 15 to 37 degrees C suggest that the dominant conformation assumed by the peptide corresponds to a coil with beta-turns in the central and C-terminal region. In line with the experiments, an increase in temperature induces structural order in the peptide, reflected by an increase in the probability for the formation of beta-turns and hydrophobic side-chain contacts, mainly in the 8-11 moiety, and to a lesser extent in the 4-7 moiety.