Chapter 2 - Multidimensional NMR of macromolecules

Abstract

This chapter presents an outline of the current state of multidimensional nuclear magnetic resonance spectroscopy and its impact on the characterization of biological macromolecules. Recent advances, particularly in heteronuclear and multidimensional nuclear magnetic resonance (NMR), made it possible to elucidate three-dimensional structures of increasingly complex proteins with remarkable precision. These developments dramatically elevated the importance of NMR in biomedical research, where many targeted proteins or nucleic acids, or protein complexes were not amenable to conventional two-dimensional proton NMR methods. Multidimensional NMR spectroscopy has evolved into a powerful, versatile analytical tool for the characterization of biomolecular structures in solution. After the conception of the basic principle of 2D NMR spectroscopy, the foundation for the geometric growth of a vast array of two and higher dimensional NMR experiments, which are applied to solve an ever growing array of analytical and structural problems, were laid. Dramatic and concurrent advances in computer technology, which provided the tools for multidimensional data processing, impressive advances in NMR spectrometer design, have facilitated the impressive growth of NMR as a research tool. The revolutionary breakthrough in biotechnology has facilitated the preparation of samples of wild type and mutant macromolecules and the incorporation of stable isotope labels into biomolecules.