Short alanine based peptides are of interest to the protein community, due, in part to their departure from the statistical coil model. These peptides are too small to assume major secondary structures, but rather, have been found to adopt an ensemble of conformations in aqueous solution, with a predominance of PPII. However, experimental evidence suggests that the presence of charged residues might induce the sampling of multiple turn conformations, thus leading to a more compact structure of the peptide. To check this further, we measured the amide I profiles of the FTIR, Raman and VCD spectrum of H-(AAKAAW)-OH, and subsequently simulated the vibrational spectra using an excitonic coupling model, with NMR coupling constant and end-to-end distance constraints. We included multiple conformations: PPII, s-strand, R helix, L helix, and turns. The alanine residues experienced a high propensity for PPII structure, ∼70%, while ∼20% for s-strand conformations and smaller percentages for other coil structures. Lysine, however showed a larger propensity for s-strand ∼30% than the alanine residues, but the PPII content for lysine is still high (∼42%). We obtained an end-to-end distance of 10A, which is in accordance with FRET measurements of the end to end distance of H-Dbo-AAKAAW)-OH, (Dbo: 2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine). This distance is indicative of a rather compact peptide sampling many different coil structures, including a high PPII content, as well as turn structures. The charge lysine residue results in more turn structures being sampled by the succeeding alanine residue. UV circular dichroism (UV-CD) spectra of H-(AAKAAW)-OH and H-(AAAAAW)-OH indicate a higher PPII content for the latter peptide. These data show that the incorporation of lysine yields indeed a more compact conformation.