Conformational properties of small, flexible peptides are a matter of ongoing interest since they can be considered as models for unfolded proteins. However, the investigation of the conformations of small peptides is challenging as they are ensembles of rapidly interconverting coil formers; moreover, the different methods used are prone to different approximations and errors. In order to obtain more reliable results, it is prudent to combine different techniques; here, molecular dynamics (MD) simulations together with nuclear magnetic resonance (NMR), fourier transform IR (FTIR), polarized Raman, and vibrational circular dichroism (VCD) measurements were used to study the conformational propensity of phenylalanine in the tripeptides AFA and GFG, motivated by the relevance of phenylalanine for the self-aggregation of peptides. The results of this analysis indicate that the F residue predominantly populate the beta-strand (beta) and polyproline II (PPII) conformations in both AFA and GFG. However, while phellylalanine exhibits a propensity for beta-strand conformations in GFG (0.40 <= beta population <= 0.69 and 0.29 <= PPII population <= 0.42), the substitution of terminal glycines with alanine residues induces a higher population of PPII (0.31 <= beta population <= 0.50 and 0.37 <= PPII population <= 0.57).