JDIT 2016 0618 021.pdf

Journal of Diagnostic Imaging in Therapy. 2016; 3(1): 7-48
http://dx.doi.org/10.17229/jdit.2016-0618-021
ISSN: 2057-3782 (Online) http://www.openmedscience.com

REVIEW ARTICLE

NMR-Active Nuclei for
Biological and Biomedical Applications
Simon G. Patchinga*
a

School of BioMedical Sciences and the Astbury Centre for Structural Molecular Biology,
University of Leeds, Leeds, LS2 9JT, UK.

(History: received 9 May 2016; accepted 25 May 2016; published online 17 June 2016)

Abstract Nuclear magnetic resonance (NMR) spectroscopy is a principal well-established technique for analysis
of chemical, biological, food and environmental samples. This article provides an overview of the properties and
applications of NMR-active nuclei (39 nuclei of 33 different elements) used in NMR measurements (solution- and
solid-state NMR, magnetic resonance spectroscopy, magnetic resonance imaging) with biological and biomedical
systems and samples. The samples include biofluids, cells, tissues, organs or whole body from different organisms
(humans, animals, bacteria, fungi, plants) for detecting and quantifying metabolites or environmental samples
(water, soils, sediments). Isolated biomolecules (peptides, proteins, nucleic acids) can be analysed for elucidation
of atomic-resolution structure, conformation and dynamics and for characterisation of ligand and drug binding, and
of protein-ligand, protein-protein and protein-nucleic acid interactions. NMR can be used for drug screening and
pharmacokinetics and to provide information in the design and discovery of new drugs. NMR can also measure
translocation of ions and small molecules across lipid bilayers and membranes, characterise structure, phase
behaviour and dynamics of membranes and elucidate atomic-resolution structure, orientation and dynamics of
membrane-embedded peptides and proteins.
Keywords: biological and biomedical applications; drug screening; dynamics; magnetic resonance imaging;
membrane proteins; metabolomics; MRI; NMR-active nuclei; nuclear magnetic resonance; protein structure

1. INTRODUCTION
1

N

UCLEAR magnetic resonance (NMR) spectroscopy is
one of the principal techniques used for analysis of
biological and biomedical systems and samples. This can
include the identification, quantification and monitoring of
ions, small molecules and biomolecules in studies of
metabolism and biological function in human and animal
cells and tissues, bacterial cells and spores, fungi and
plants. Similar types of measurements can be performed on
environmental samples such as water, soils and sediment.

OPEN ACCESS PEER-REVIEWED
*Correspondence E-mail: s.g.patching@leeds.ac.uk
Citation: Patching SG. NMR-Active Nuclei for Biological and
Biomedical Applications. Journal of Diagnostic Imaging in Therapy.
2016;3 (1): 7-48.
http://dx.doi.org/10.17229/jdit.2016-0618-021
Copyright: © 2016 Patching SG. This is an open-access article distributed
under the terms of the Creative Commons Attribution License (CC By
4.0), which permits unrestricted use, distribution, and reproduction in any
medium, provided the original author and source are cited.

NMR is able to elucidate atomic-resolution structure,
conformation, molecular mechanism, dynamics and
exchange processes (on timescales of picoseconds to
seconds) in biomolecules, especially peptides, proteins and
nucleic acids. NMR can be used for the observation,
quantification and characterisation of ligand and drug
binding to biomolecules, and for characterisation of ligandprotein, protein-protein and protein-nucleic acid
interactions. NMR can be used for drug screening and it
can acquire structural, binding and kinetic information for
the design and discovery of new drugs. It can then monitor
the absorption, distribution, metabolism and excretion
(ADME) of administered drugs in pharmacokinetics
studies.
NMR can be used for the observation,
quantification and kinetic characterisation of ion and smallmolecule translocation across lipid bilayers and biological
membranes, including those of cells, tissues and vesicles.
Solid-state NMR in particular can investigate the
interactions and effects of peptides, proteins and small
molecules on the structure, phase behaviour and dynamics
7