Elsevier

Chemical Physics Letters

Volume 398, Issues 4–6, 11 November 2004, Pages 522-525
Chemical Physics Letters

Backbone dynamics in collagen

https://doi.org/10.1016/j.cplett.2004.09.114Get rights and content

Abstract

Peptide backbone motions of collagen have been extensively studied in the past. The experimental results were interpreted using a model of a collagen rod librating about its helix axis. Considering the size of the collagen molecule and the presence of cross-linked molecules, motional amplitudes derived for the helix axis libration were unusually high. Using solid-state NMR 13C chemical shift anisotropy and 2H quadrupolar lineshape analysis for five different isotope labelled collagens we show that motional averaging of the NMR interactions occurs primarily via small-angle librations about internal bond directions. This type of dynamics is compatible with both the presence of cross-links in collagen and the X-ray data, as well as dynamic models used for other proteins.

References (26)

  • S.K. Sarkar et al.

    J. Biol. Chem.

    (1983)
  • J.A. Rupley et al.

    Adv. Prot. Chem.

    (1991)
  • N.D. Lazo et al.

    J. Magn. Reson. Ser. B

    (1995)
  • L.W. Jelinsky et al.

    Nature

    (1980)
  • L.W. Jelinsky et al.

    Biophys. J.

    (1980)
  • S.K. Sarkar et al.

    Biochemistry

    (1985)
  • D.A. Torchia

    Ann. Rev. Biophys. Bioeng.

    (1984)
  • R.D.B. Fraser et al.

    Biosci. Rep.

    (1986)
  • R. Berisio et al.

    Protein Sci.

    (2002)
  • R.Z. Kramer et al.

    Nat. Struct. Biol.

    (1999)
  • M. Demura et al.

    J. Am. Chem. Soc.

    (1998)
  • W.H. Press et al.

    Numerical Recipes in FORTRAN: The Art of Scientific Computing

    (1992)
  • A.E. Aliev et al.

    Magn. Reson. Chem.

    (1998)
  • Cited by (8)

    View all citing articles on Scopus
    View full text