Solving solution structures of physiologically relevant proteins by NMR spectroscopy.

Abstract

In the last decade or so, high resolution nuclear magnetic resonance (NMR) spectroscopy has become the technique of choice to study protein solution structure and dynamics at the molecular level. This is due, in part, to much improved instrumentation, but it is principally the consequence of the de­ velopment of two-dimensional NMR methodologies. The latter were first proposed by Jeener in the early 1970s (56) and were vigorously applied to protein structural analysis some ten years later, initially by Wuthrich and his co-workers (134). Since then many groups have further developed NMR methodologies and applied them to the study of structure and dynamics of a wide array of proteins (see, for example, 9, 80, 129, 30, 57 for more recent reviews) and other macromolecules. This chapter briefly summarizes the NMR protocol for the eventual realiza­ tion of the three-dimensional solution structure of physiologically relevant proteins given the restraints of the NMR technique. Because of space limita­ tions, this article is not exhaustive, and many fine studies are not mentioned in detail or at all (for example, 32). We have chosen to concentrate on families of related proteins on which detailed NMR structural analyses have been performed.