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New techniques in structural NMR — anisotropic interactions

Nature Structural Biology volume 5, pages 517–522 (1998)Cite this article

Abstract

Structure determination of biomolecules by NMR has traditionally been based on nuclear Overhauser effects (NOEs). Now there are additional sources of information that can complement NOEs in cases where positioning of remote parts of molecules is important, and where extension to larger and more complex systems is desired.

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Figure 1: Dipolar coupled 15N-1H spin pair in an amide bond.
Figure 2: Induced protein orientation by dilute phospholipid bicelles.
Figure 3: Segments from a proton coupled, nitrogen decoupled, 15N-1H HSQC spectrum of a 0.4 mM solution of a barley lectin fragment in a 5% DMPC/DHPC 3:1 bicelle (doped with a positively charged amphiphile).
Figure 4: Chemical shift anisotropy of an amide carbonyl carbon.
Figure 5: Properly oriented domains in a two zinc-finger–DNA complex have common orientations of independently determined principle orientation tensors.
Figure 6: Line widths for the two lines of a proton coupled 15N doublet as a function of spectrometer operating frequency.

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Acknowledgements

Support from the NIH and NSF is gratefully acknowledged. We also thank J. Losonczi, A. Fowler, M. Fischer and H. Al-Hashimi for their help in preparing the figures.

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  1. the Complex Carbohydrate Research Center, University of Georgia, Athens, 30602-4712, Georgia, USA

    J.H. Prestegard

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Correspondence to J.H. Prestegard.

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Prestegard, J. New techniques in structural NMR — anisotropic interactions. Nat Struct Mol Biol 5 (Suppl 7), 517–522 (1998). https://doi.org/10.1038/756

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