The tools of structural biology provide beautifully detailed snapshops of the lowest energy (or most readily crystalizable) protein conformation, but offer precious little in the way of dynamic information. Since many aspects of protein function (i.e. substrate binding/release, conformational changes, energy dissipation through bond vibrations etc.) are inherently dynamic, a detailed understanding of the dynamic modes available to proteins is required to accurately predict their functional characteristics. Very recently, there have been a number of exciting advances in analytical biochemistry that permit detailed studies of protein dynamics. In particular, CPMG relaxation dispersion NMR and Time Resolved ESI-MS (a technique introduced by Dr. Wilson during his Ph.D. under Dr. Lars Konermann) facilitate studies of protein conformational dynamics on the biologically important millisecond timescale. In our research, we use these techniques, together with microfluidics and basic biochemistry, to characterize the dynamics underlying activity in a number of enzyme systems. We also develop novel approaches for microfluidic coupled MS and NMR-based investigations.