Chapter 7 - Nuclear Magnetic Resonance

Abstract

This chapter focuses on the application of high-resolution multidimensional nuclear magnetic resonance (NMR) methods to determine the structures of proteins and nucleic acids in a solution. Comprehension of biological processes at the molecular level requires knowledge of the three-dimensional structures of the molecules involved, the dynamic properties of the molecules, and the intermolecular interactions in which the molecules participate. X-ray diffraction and NMR spectroscopy are the two methods that are available for determining three-dimensional structures of proteins and nucleic acids at the level of atomic resolution. Using NMR, molecules can be examined in a solution under near-physiological conditions where effects of solvent composition, pH, temperature, and other factors on structure can be probed. Dynamic processes occurring over a wide range of time scales (picoseconds–seconds) can be examined by NMR methods as well. These characteristics have made NMR an alternative to X-ray crystallography for determination of a biomolecular structure. The highly localized nature of NMR in which a nucleus is affected by influences in its immediate vicinity and the sensitivity of NMR parameters to dynamic processes occurring over a very wide range of time scales can provide unique structural and dynamic information not available from other spectroscopic methods.