Fluorine Magnetic Resonance in Biochemistry

Proton magnetic resonance (PMR) spectroscopy has proved to be an important tool in structural studies of biological macromolecules (Roberts and Jardetzky, 1970; Casy, 1971; Jardetzky and Wade-Jardetzky, 1971; Dwek, 1973; James, 1975; Wuthrich, 1976; Thomas, 1976). The magnetic fields currently available can provide resonance frequencies of 360 MHz or higher, and with the spectral dispersion available under these conditions, PMR is often the method of choice for examining small proteins and peptides in solution. In these situations it is usually possible to assign many of the signals observed to specific amino acids and thus have available a number of spectroscopic probes into the structure of the molecule; we take “structure” in this context to include not only sequence information but also details of conformational motions.