I became involved in a project in the fall of 1994, with the goal learning more about the exact physical interactions that stabilize protein-RNA complexes. The protein we were interested in was called U1A, and using simple Fluorine-19 1-D NMR techniques, we were hoping to find out more about what features of the protein allow it to bind successfully and specifically to this DNA domain. Our ultimate goal was to use the structural information we gain from the spectra of the native complex to redesign the U1A protein so that it binds to a different DNA domain. My project involved inducing a population of bacteria containing a plasmid with the gene for a U1A-MBP (maltose binding protein) fusion protein, to produce that protein. I then attempted to purify the protein using affinity chromatography, cleave it from the MBP domain, and purify each fragment. The purification steps proved to be much more complex/difficult than we had anticipated, and this is where the semester (and my project) ended. I did learn a lot, though, and it was a great experience, to express my first protein. :-)