There have been ALC studies on the interaction of muons with native proteins, but little systematic work that contributes understanding of how spectroscopic information alters with structure. However, to truly understand the applicability of the ALC method to native material one has tounderstand the limitations of the method in such complex bio-polymers. To test these limits, we wish to build on our phenylalanine study and use a short peptide that forms an alpha-helical structure. Using the sequence, Glu-Leu-Glu-Lys-Glu-Leu-Glu-Lys-Lys-Phe, we expect muonaddition to the Phe ring and C=0 species (backbone) only. By already studying coupling to Phe, we will be able to understand how addition of this acid to a C=O rich sequence alters the Phe resonance, understand the resonance signature from those muons tagging the backbone andmonitor both in the folded and unfolded state