Solid State Nuclear Magnetic Resonance has moved to the forefront of spectroscopic techniques to elucidate the structure and dynamics of a protein in a restricted state. The methodological development in the instrumentation and pulse sequence design has allowed the true benefits of working with solids using NMR to be realized. In this thesis three different NMR probes will be highlighted which showcase the unique problems that are solved as a result. First, the problems associated with the implementation of a computational step using the spins for quantum information processing will be explored. As it turns out, there exists decoherent behavior or losses of information during the processing steps that have been addressed and will be discussed. From here the gears will be switched to explore the establishment of a protocol for delineating the complete assignment of the back-bone and side-chain of a protein will be highlighted along with the development from both the theoretical side along with the instrumentation side will be discussed.

Finally, as a result of the improvements in both of the previously highlighted applications the attempt to generate an electric field across a sample while immersed in an NMR receiver coil will be explored with the ultimate goal of observing the NMR spectral signature. After highlighting these three applications the ability to utilize the methods of solid-state NMR should be completely realized as a result.