Abstract
With the widespread utilization of Fourier transform (F1) and high field nuclear magnetic resonance (NMR) spectrometers, 31 P NMR spectroscopy of biological phosphates has now become quite common. This is not surprising, since the 31p nucleus has convenient NMR properties: spin 1/2, 100% natural abundance, moderate relaxation times, wide range of chemical shifts, and a key role in many biomolecu lar structures. Fourier transform NMR has substantially reduced the one serious limitation to the use of 31p NMR in biological systems, which is the low sensitivity of the phosphorus nucleus (6.6% at constant field compared to IH NMR). Routinely, millimolar (or lower) con centrations of phosphorus nuclei are conveniently monitored. NMR spectroscopic information includes the resonant line positions (chemical shifts, 8), the spin-spin coupling constants (J), and spin-lattice (TI) and spin-spin (1;) relaxation times. In addition, signal areas are often directly related to nuclei concentration. With these parameters NMR spectroscopy provides a unique, nonperturbing probe in solution of the structure and time-dependent properties of molecules. Much of this review is concerned with 31p chemical shifts. Effective use of 31p NMR as a probe of nucleotide conformation requires an understanding of the structural and environmental factors that influence these shifts. I will therefore first discuss some of the factors that alter
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