Abstract
It has been clear since the first NMR spectra of proteins that chemical shifts contain a lot of information on protein structure. In denatured proteins, most nuclei resonate at frequencies similar to those observed in small peptides, and therefore show a considerable degree of overlap and a lack of spectral dispersion, whereas in folded proteins some signals are shifted markedly. The chemical shift range spanned by nuclei within the same covalent framework is enormous compared to the accuracy with which they can be measured; thus, 1Hα shifts for each amino acid span a range of approx 2 ppm around the average position, 13Cα approx 8 ppm, 13C′ (carbonyl carbons) approx 5 ppm, 15N about 20 ppm, and 19F about 15 ppm, whereas they can be measured to an accuracy of 0.05 ppm or better. However, it is only in the last few years that it has been possible to use the chemical shifts in a reliable way. This is partly because computers are now much faster, but mostly because it is only recently that large numbers of chemical shift assignments have become available, for proteins with known three-dimensional (3D) structure. As a result, it has been possible to compare calculations to experiment, and therefore to reach a deeper understanding of the origins of the chemical shift, and refine the equations used. Thus, as discussed herein, it is now possible not only to calculate chemical shifts from structures, but also to derive structural constraints from chemical shifts.
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© 1997 Humana Press Inc.
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Williamson, M.P., Asakura, T. (1997). Protein Chemical Shifts. In: Reid, D.G. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 60. Humana Press. https://doi.org/10.1385/0-89603-309-0:53
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DOI: https://doi.org/10.1385/0-89603-309-0:53
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