NMR Methodology Development
The ability to probe the amplitude and timescale of molecular motion is important; as such processes influence chemical transformations. Nuclear magnetic resonance (NMR) spectroscopy is particularly well-suited for the characterization of molecular motion at a wide range of time scales. While many NMR methods exist for the characterization of molecular motions that occur on the µs-ms timescale, such techniques are quite laborious and expensive to perform. This is particularly true for slow tumbling molecules with low sensitivity, as is the case with proteins. Our laboratory has been working on the development of more simplistic methods to probe chemical exchange processes by NMR spectroscopy, with a focus on the ability to characterize small molecules (for instance, NN-dimethylforamide) that were first used to develop staple approaches such as the Carr-Purcell-Meiboom-Gill (CPMG) block, and further apply this to model protein systems that experience a variety of timescales for chemical exchange.