Gas-Phase NMR Spectroscopy

Nuclear Magnetic Resonance (NMR) spectroscopy has become one of the most powerful tools available to the chemist and biochemist for the study of structure and chemical exchange in a multitude of chemical systems. The phenomenon of nuclear magnetic resonance was first observed in 1946, and in these last five decades the field has grown tremendously. Today, almost every university chemistry department owns at least one commercial NMR spectrometer. Historically, the development of both the experimental and theoretical backbone of NMR has been tied to high-resolution NMR spectroscopy of isotropic liquids or solutions. Even after fifty years, the pace at which solution NMR data is presented in the literature remains staggering. The Protein Data Bank at Brookhaven National Laboratory alone holds NMR files describing almost one thousand proteins, peptides, and viruses, and over 500 different multidimensional pulse sequences have been published describing the acquisition methods for the determination of three-dimensional structures in solution.