Abstract

Multidimensional nuclear magnetic resonance (NMR) has proven to be a valuable tool for establishing the structure and dynamics of biological molecules in solution. Solution NMR is frequently combined with X-ray diffraction and molecular mechanics calculations to determine the extent to which solution properties are retained in the solid state. However, many biological molecules cannot be prepared as single crystals. In addition, the presence of solvent may have a profound effect on the structure and dynamics of individual molecules, and change the nature of intermolecular interactions. Solution techniques are not adequate for the examination of molecules or assemblies of molecules in which motion is restricted, so that isotropic tumbling fast on the NMR time scale does not occur. Techniques applied to study solid samples of Synthetic polymers and inorganic glasses can be applied to questions of biological interest. This chapter outlines the differences between nuclear interactions in solution and in the solid state, and then introduces the techniques commonly used to obtain useful spectra from solid samples. A number of applications are presented in which information uniquely available from solid-state NMR has increased our understanding of a biological material or process. The wide scope of this chapter precludes a complete listing of all related research.

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