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An introduction to biological nuclear magnetic resonance spectroscopy
Author(s) -
Bothwell John H. F.,
Griffin Julian L.
Publication year - 2011
Publication title -
biological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.993
H-Index - 165
eISSN - 1469-185X
pISSN - 1464-7931
DOI - 10.1111/j.1469-185x.2010.00157.x
Subject(s) - nuclear magnetic resonance spectroscopy , spectroscopy , nuclear magnetic resonance , chemistry , two dimensional nuclear magnetic resonance spectroscopy , nmr spectra database , fluorine 19 nmr , nuclear magnetic resonance crystallography , relaxometry , transverse relaxation optimized spectroscopy , chemical physics , analytical chemistry (journal) , spectral line , physics , spin echo , magnetic resonance imaging , chromatography , medicine , quantum mechanics , astronomy , radiology
Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful analytical techniques available to biology. This review is an introduction to the potential of this method and is aimed at readers who have little or no experience in acquiring or analyzing NMR spectra. We focus on spectroscopic applications of the magnetic resonance effect, rather than imaging ones, and explain how various aspects of the NMR phenomenon make it a versatile tool with which to address a number of biological problems. Using detailed examples, we discuss the use of 1 H NMR spectroscopy in mixture analysis and metabolomics, the use of 13 C NMR spectroscopy in tracking isotopomers and determining the flux through metabolic pathways (‘fluxomics’) and the use of 31 P NMR spectroscopy in monitoring ATP generation and intracellular pH homeotasis in vivo . Further examples demonstrate how NMR spectroscopy can be used to probe the physical environment of a cell by measuring diffusion and the tumbling rates of individual metabolites and how it can determine macromolecular structures by measuring the bonds and distances which separate individual atoms. We finish by outlining some of the key challenges which remain in NMR spectroscopy and we highlight how recent advances—such as increased magnet field strengths, cryogenic cooling, microprobes and hyperpolarisation—are opening new avenues for today's biological NMR spectroscopists.