Principles of Nuclear Magnetic Resonance and Selected Biological Applications

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Nuclear Magnetic Resonance (NMR) spectroscopy is extremely powerful to study distinct biological systems ranging from biomolecules to specific metabolites. This chapter presents the basic concepts of the technique and illustrates its potential to study such systems. Similarly, to other spectroscopic techniques, the theoretical background of NMR is sustained by detailed mathematics and physical chemistry concepts, which were kept to the minimum. The intent is to introduce the fundamentals of the technique to science students from different backgrounds. The basic concepts of NMR spectroscopy are briefly presented in the first section, and the following sections describe applications in the biosciences field, using electron transfer proteins as model, particularly cytochromes. The heme groups endow cytochromes with particular features making them excellent examples to illustrate the high versatility of NMR spectroscopy. The main methodologies underlying protein solution structure determination are discussed in the second section. This is followed by a description of the main experiments explored to structurally map protein-protein or protein-ligand interface regions in molecular complexes. Finally, it is shown how NMR spectroscopy can assist in the functional characterization of multiheme cytochromes.
Original languageEnglish
Title of host publicationRadiation in Bioanalysis: Spectroscopic Techniques and Theoretical Methods
EditorsA. Pereira, P. Tavares, P. Limão-Vieira
Place of PublicationCham
ISBN (Electronic)978-3-030-28247-9
ISBN (Print)978-3-030-28247-9
Publication statusE-pub ahead of print - 22 Sep 2019

Publication series

NameBioanalysis (Advanced Materials, Methods, and Devices)
ISSN (Print)2364-1118


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