Introduction
Among the many spectroscopic methods which can be used to study the structure and dynamics of proteins, NMR, while originating in the somewhat recondite phenomenon of nuclear spin angular momentum, has proved to be arguably the most powerful. The power of the method in the study of proteins results largely from the fact that nuclei of the same element in different chemical and magnetic environments give rise to distinct spectral lines (the chemical shift), so that – even in as complex a molecule as a protein – information can be obtained at the level of individual atoms. Furthermore, NMR is sensitive to both the structure and dynamics of molecules as well as their interactions. This has led to an enormous growth in the application of NMR to the study of biological macromolecules since the tentative beginnings some 50 years ago. In the words of Emsley and Feeney (1995): “NMR started as the plaything of the physicists, became the favourite toy of the chemists and finally...
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Roberts, G.C.K. (2013). Protein NMR – Introduction. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_303
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DOI: https://doi.org/10.1007/978-3-642-16712-6_303
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