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Cartilage and Osteoarthritis pp 303–318Cite as

Dynamics of Collagen in Articular Cartilage Studied by Solid-State NMR Methods

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Part of the book series: Methods in Molecular Medicine ((MIMM,volume 101))

Abstract

Methods for studying the fast molecular dynamics of the rigid macromolecules in cartilage are described. The strong dipolar couplings and chemical shift anisotropies of these molecules necessitate application of solid-state nuclear magnetic resonance (NMR) techniques such as magic-angle spinning, cross-polarization, and high-power dipolar decoupling to obtain resolved NMR spectra. The molecules in cartilage that are amenable to these techniques are collagen and the rigid portion of the glycosaminoglycans (mostly hyaluronan). Site-specific mobility information is obtained from scaled dipolar couplings measured in 2D NMR experiments. Motionally averaged dipolar couplings can be interpreted in terms of order parameters that provide information about the amplitudes of molecular motions. Qualitative dynamics information is obtained from the simple wideline separation experiment measuring 1H-1H widelines representing the strength of the 1H-1H dipolar coupling. Quantitative values for molecular order parameters are obtained from precise measurements of 1H-13C dipolar couplings along the C-H bond vector. Two experimental techniques, the Lee-Goldburg cross-polarization and the dipolar coupling/chemical shift experiment, are illustrated to measure these 1H-13C dipolar couplings. Unlike glycosaminoglycans in cartilage, the collagen moiety remains substantially ordered, undergoing fast small amplitude motions. As enzymes cleave the macromolecules in articular cartilage in the course of arthritis, solid-state NMR techniques are capable of characterizing the increased motions of their degradation products in diseased cartilage.

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Author information

Authors and Affiliations

  1. Junior Research Group “Solid-state NMR Studies of the Structure of Membrane-Associated Proteins,” Biotechnological Biomedical Center/Institute of Medical Physics and Biophysics, Medical Department, University of Leipzig, Leipzig, Germany

    Daniel Huster

  2. Institute of Medical Physics and Biophysics, Medical Faculty, University of Leipzig, Leipzig, Germany

    Jürgen Schiller

  3. Institute of Medical Physics and Biophysics, Medical Department, University of Leipzig, Leipzig, Germany

    Klaus Arnold

Authors
  1. Daniel Huster
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  2. Jürgen Schiller
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  3. Klaus Arnold
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Editor information

Editors and Affiliations

  1. Division de Rhumatologie, Institut de Recherches Servier, Suresnes, France

    Frédéric De Ceuninck , Massimo Sabatini  & Philippe Pastoureau ,  & 

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© 2004 Huaman Press Inc., Totowa, NJ

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Huster, D., Schiller, J., Arnold, K. (2004). Dynamics of Collagen in Articular Cartilage Studied by Solid-State NMR Methods. In: De Ceuninck, F., Sabatini, M., Pastoureau, P. (eds) Cartilage and Osteoarthritis. Methods in Molecular Medicine, vol 101. Humana Press. https://doi.org/10.1385/1-59259-821-8:303

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  • DOI: https://doi.org/10.1385/1-59259-821-8:303

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-505-7

  • Online ISBN: 978-1-59259-821-2

  • eBook Packages: Springer Protocols

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