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Nuclear Magnetic Resonance Spectroscopy

  • Thomas C. PochapskyEmail author
  • Susan Sondej Pochapsky
Chapter
Part of the Biophysics for the Life Sciences book series (BIOPHYS, volume 6)

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.

Keywords

Stable isotopes TROSY Nuclear Overhauser effect Dipolar coupling Solid-state NMR Protein Nucleic acid Deuteration 

Notes

Acknowledgment

Both authors acknowledge partial support from NIH grant R01-GM44191.

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© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of Chemistry and Rosenstiel Basic Medical Sciences Research InstituteBrandeis UniversityWalthamUSA

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