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Applicability and Limitations of Three-Dimensional NMR Spectroscopy for the Study of Proteins in Solution

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Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy

Part of the book series: NATO ASI Series ((NSSA,volume 225))

Abstract

Assignment procedures for backbone resonances of proteins are outlined for homonuclear and heteronuclear three-dimensional NMR spectroscopy. Phasecycling procedures in fast 3D experiments are discussed. Examples of data space reducing processing techniques are given. A new triple resonance based assignment procedure for protein resonances is outlined. The general advantages and disadvantages of homonuclear and heteronuclear three-dimensional NMR spectroscopy are discussed.

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Author information

Author notes

  1. Erik R. P. Zuiderweg

    Present address: Biophysics Research Division, University of Michigan, 2200 Bonisteel Blvd., Ann Arbor, MI, 48109, USA

Authors and Affiliations

  1. Department of Chemistry, University of Utrecht, Padualaan 8, 3584, CH Utrecht, The Netherlands

    Rolf Boelens

  2. Institute for Organic Chemistry, Johann Wolfgang Goethe University, Niederurseler Hang, 6000, Frankfurt-am-Main 50, Federal Republic of Germany

    Christian Griesinger

  3. NIDDK, National Institutes of Health, Laboratory of Chemical Physics, Bld. 2, Bethesda, MD, 20892, USA

    Lewis E. Kay

  4. Centre de Biophysique Moleculaire, C.N.R.S., F-45071, Orleans Cedex 2, France

    Dominique Marion

  5. Pharmaceutical Discovery, Abbott Laboratories, Abbott Park, IL, 60064, USA

    Erik R. P. Zuiderweg

Authors
  1. Rolf Boelens
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  2. Christian Griesinger
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  3. Lewis E. Kay
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  4. Dominique Marion
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  5. Erik R. P. Zuiderweg
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Editor information

Editors and Affiliations

  1. Rowland Institute for Science, Cambridge, Massachusetts, USA

    Jeffrey C. Hoch

  2. Carlsberg Laboratory, Copenhagen, Denmark

    Flemming M. Poulsen

  3. University of Oxford, Oxford, England

    Christina Redfield

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© 1991 Springer Science+Business Media New York

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Boelens, R., Griesinger, C., Kay, L.E., Marion, D., Zuiderweg, E.R.P. (1991). Applicability and Limitations of Three-Dimensional NMR Spectroscopy for the Study of Proteins in Solution. In: Hoch, J.C., Poulsen, F.M., Redfield, C. (eds) Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy. NATO ASI Series, vol 225. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9794-7_9

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  • DOI: https://doi.org/10.1007/978-1-4757-9794-7_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9796-1

  • Online ISBN: 978-1-4757-9794-7

  • eBook Packages: Springer Book Archive

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