Src Kinase is a protein of tyrosine kinases family. This protein is composed of four sites: an SH2 and SH3 domain, an active site and catalytic site. These domains transmit signals from the plasma membrane to other cells. Inhibitors of Src Kinase typically bind the SH2 domain and the active site in a bivalent fashion. Our overall goal is to investigate how this process occurs using spectroscopic measurements. To model some of the plausible interactions that might exist between the protein Src Kinase and its inhibitor, we determined the fluorescence emission and excitation spectra for two amino acids and two peptides. We took the fluorescence spectra of phosphotyrosine and pentafluorophenylalanine in water, methanol, acetonitrile, and chloroform to investigate the effect of polarity, and dimethyl sulfoxide (DMSO) for an aprotic environment. Due to limited solubility problems the peptides where only run in water and DMSO. To help analyze our results, we did some Gaussian 03W calculations to estimate the electronic spectra of each molecule. Comparison of the data collected in water, methanol, acetonitrile, and chloroform, revealed that while the excitation peaks where not significantly shifted, the emission peaks were. In DMSO, the excitation peaks were red shifted while the emission peaks were blue shifted. Our data was analyzed in terms of the sensitivity of these peaks to its environment.