Abstract
Nuclear magnetic resonance (NMR) has developed into an important tool for investigating the structure and dynamics of biomacromolecules in solution, associated with membranes and in solids. This chapter provides an introduction to the theory of NMR and a description of basic concepts (excitation of NMR transitions, spin populations and coherence, relaxation phenomena, signal detection and processing). Types of structural and dynamic information available from NMR experiments are noted. Standard experiments used for sequential assignment of resonances in biomolecules in solution and solid state are discussed, along with instrumentation and sample requirements. In particular, the need for selective and uniform isotope labeling is detailed. Software used to process NMR data and generate structural and dynamic information are noted, and data needed for structure determinations and dynamic analysis outlined.
All references to commercially available products and software are for the reader’s convenience and information only. No guarantees of product safety, availability, comprehensiveness of listings or completeness of descriptions/pricing are made or implied.
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Both authors acknowledge partial support from NIH grant R01-GM44191.
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Pochapsky, T.C., Pochapsky, S.S. (2013). Nuclear Magnetic Resonance Spectroscopy. In: Allewell, N., Narhi, L., Rayment, I. (eds) Molecular Biophysics for the Life Sciences. Biophysics for the Life Sciences, vol 6. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-8548-3_5
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