I have spent the past decade using Nuclear Magnetic Resonance NMR) spectroscopy to study the structure, interaction and dynamics of molecules ranging from 50 to 50,000 Daltons in size. As an undergraduate, I used 2D NMR to study how various solvent conditions would affect the structure and dynamics of peptides and other small molecules. In graduate school I studied protein evolution, using 3D NMR to probe for structural changes as the sequence of an ancetral protein is mutated towards its descendant. During a brief postdoc, I have worked on optimizing a 4D NMR pulse sequence to study interactions within large protein systems, before returning to UA to pursue my passion for teaching. In my training as an NMR spectroscopist, I have experienced the different approaches taken by organic chemists and structural biologists. Now as an instructor and an assistant staff scientist at the NMR facilty, I aim to share these skills by teaching hands-on NMR courses and providing guidance to our researchers.