[ACCESS RESTRICTED TO THE UNIVERSITY OF MISSOURI SYSTEM AT REQUEST OF AUTHOR.] The Ribosome is a fundamental molecular machine found in all cells and is responsible for synthesizing proteins.(Lehninger Principles of Biochemistry 5th Edition) Determining the mechanism underlying ribosome function is of interest to a large number of research laboratories around the world. The Cornish laboratory at MU has recently identified inter subunit rotational states related to specific steps of the protein synthesis cycle.(Cornish P, 2008) Following up on this recent work, I set out to study conformational dynamics of the ribosome at the single molecule level. In particular, I wanted to learn about how the rotational states of ribosome identified would be modulated by varying the ionic strength of the buffer solution. In order to execute this research, I needed to learn a number of biochemical techniques as well as how to operate a state-of-the-art total internal reflection microscope capable of observing the florescence signal generated by a single molecule. Overcoming technical aspects of the project turned out to be more time consuming that I originally thought. Indeed, the bulk of my M.S. thesis work was taken up trouble shooting a number of sample preparation protocols, benchmark samples, as well as instrumentation. That said, I was able to observe smFRET from a few ribosome samples, but the project came up short in my effort to study the salt concentration dependence of the inter subunit rotational states of the ribosome.