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The Proton Magnetic Resonance Spectroscopy of Proteins

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Natural and Synthetic High Polymers

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Abstract

Ideally we would like to derive from investigations of proteins in solution the same structural details which X-ray diffraction methods have yielded for the crystalline state. Of the spectroscopic methods perhaps nuclear magnetic resonance has the greatest potential since, in principle, 1H and 13C nuclear magnetic resonance spectra are dependent on the properties of all amino acid components. The parameters which describe NMR spectra provide a wealth of information on each magnetic nucleus. The chemical shift is sensitive to the electronic and molecular environment; the area of each resonance is proportional to the number of nuclei involved; the fine structure, characterised by coupling constants, describes interactions with neighbouring magnetic nuclei and the nuclear spin relaxation times, T 1 and T 2, depend on inter- and intramolecular magnetic dipole interactions. Unfortunately it is not always, indeed it is seldom, possible to extract this wealth of information from the NMR spectra of proteins due to certain inherent difficulties. The method is insensitive though this can be overcome at least for small (M. W. < 25.000) proteins, by the use of computers to accumulate and average the spectra. The use of spectrometers employing high frequencies should also improve the sensitivity whilst Fourier-transform-NMR [1] is of considerable promise, particularly for the study of 13C nuclei.

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Author information

Authors and Affiliations

  1. Inorganic Chemistry Laboratory, Oxford, England

    H. A. O. Hill

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  1. H. A. O. Hill
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Editor information

Editors and Affiliations

  1. Physikalisches Institut, Universität Basel, Germany

    P. Diehl

  2. Institut für Anorganische Chemie, Universität Stuttgart, Germany

    E. Fluck

  3. Institut für Physikalische Chemie, Rhein.-Westf. Technischen Hochschule Aachen, Germany

    R. Kosfeld

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© 1971 Springer-Verlag Berlin Heidelberg

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Hill, H.A.O. (1971). The Proton Magnetic Resonance Spectroscopy of Proteins. In: Diehl, P., Fluck, E., Kosfeld, R. (eds) Natural and Synthetic High Polymers. NMR Basic Principles and Progress / NMR Grundlagen und Fortschritte, vol 4. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-65089-5_10

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  • DOI: https://doi.org/10.1007/978-3-642-65089-5_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-65091-8

  • Online ISBN: 978-3-642-65089-5

  • eBook Packages: Springer Book Archive

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