Abstract
Ring current effects are the major source of conformation-dependent shifts observed in the 1H NMR spectrum of proteins, diamagnetic hemeproteins, or transfer RNAs. NMR spectroscopic techniques are nowadays capable of characterizing protein or transfer RNA spectra in great detail, especially in the case of small proteins (Campbell and Dobson, 1979). X-ray analyses of proteins or transfer RNAs have also attained sophisticated levels of crystallographic refinement in recent years (Blundell and Johnson, 1976; Artymiuk et al.,1979). Spectroscopic results can therefore be interpreted in terms of structural interactions based on the local environment of the aromatic ring in the macromolecule. These act as quite natural probes of the structure. Ring current concepts provide, directly or indirectly, a link between spectroscopy and structure in both static and dynamic aspects. Accordingly they constitute an invaluable key for appreciation of the significant biological properties of macromolecules from 1H NMR studies. This review chapter examines this role in detail, firstly to base this on the aromatic rings in proteins and then to extend this to transfer RNA. Since it is also the purpose of this chapter to assist the reader to see where ring current concepts can be applied, to perform his or her own calculations, and to be able to interpret ring current effects, details are given to facilitate this.
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Perkins, S.J. (1982). Application of Ring Current Calculations to the Proton NMR of Proteins and Transfer RNA. In: Berliner, L.J., Reuben, J. (eds) Biological Magnetic Resonance. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6540-6_4
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