In only seven decades since the development of penicillin, antibiotic resistance has become a widespread problem of the modern world to which only few solutions currently exist. The fast paced rhythm of evolution in the world of bacteria is surpassing the rate of drug discovery, with MRSA (a strain of S. aureus resistant to methicillin, a second generation Ì_å_-lactam antibiotic) being one of the favorites in the race. Responsible for this resistance are the sensing/transducing systems BlaR and MecR. Upon interaction with the Ì_å_-lactam antibiotic through its surface domain, BlaR initiates the signal transduction process. This event leads to the activation of the cytoplasmic domain, with the final result of de-repression of blaZ, the Ì_å_ lactamase encoding gene. As shown by Mobashery et al. [1], the signal transduction process involves conformational changes of the cell surface sensor domain of the BlaR protein upon ligand binding. This prompts the need to look at the dynamics necessary to the signaling mechanism. Nuclear Magnetic Resonance (NMR) is a spectroscopic technique that provides an atomic resolution description of the system of interest and allows for the study of both protein structure and dynamics. However, many interesting and biologically relevant proteins pose experimental difficulties due to their large molecular weights and poor stability in a highly concentrated solution state. Practical solutions to these experimental concerns will be detailed within this thesis. The focus of this study will be the novel characterization of the S. aureus BlaR sensor domain, BlaRs (30KDa). Contained within this thesis will be the initial characterization of BlaR with NMR in both the free and antibiotic bound form. These results provide the first atomic resolution study of BlaRs and its associated signaling mechanism in the solution state, and supply initial data required for future studies.