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The second decade — into the third millenium

Abstract

NMR spectroscopy is one of the principal experimental techniques of structural biology, with abilities to determine atomic resolution structures as well as investigate dynamics and intermolecular interactions of biological macromolecules. There is plenty of room for continued progress of this young branch of science, based on further technical advances as well as innovative funding strategies and project organization.

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Figure 1: NMR structure of the recombinant murine prion protein.
Figure 2: Frequency dependence from 100–1800 MHz of the full resonance line width at half height for amide groups in TROSY experiments calculated for three correlation times of τc = 20, 60 and 320 ns, which represent spherical proteins with molecular weights of 50,000, 150,000 and 800,000 Mr.
Figure 3: Comparison of conventional and TROSY-type 15N-1H correlation spectra of the uniformly 15N- and 2H-labeled 110,000 Mr protein 7,8-dihydroneopterin aldolase from Staphylococcus aureus in H2O solution.

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Acknowledgements

Support by the Schweizerischer Nationalfonds is gratefully acknowledged. The author thanks K. Pervushin, R. Riek and G. Wider for the preparation of the figures and for discussions.

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Wüthrich, K. The second decade — into the third millenium. Nat Struct Mol Biol 5 (Suppl 7), 492–495 (1998). https://doi.org/10.1038/728

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