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Refolding of Collagen IV and Other Collagens as Monitored by Electron Microscopy

  • R. Dölz
  • J. Engel
  • K. Kühn
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 3)

Abstract

In vivo, the formation of the triple helical structure is one of the important post translational events leading to the collagen precursor molecule. A prerequisite for the correct folding to an intact triple helix is a correct alignment and association of three polypeptide chains. As demonstrated for collagen I and III (Bächinger et al., Eur. J. Biochem. (1980) 106, 619; Bruckner et al., Eur. J. Biochem. (1978) 90, 595) this is facilitated by carboxyterminal crosslinks or peptides. The mechanism of collagen folding was described by a zipper model which proceeds from the C- to the N- terminus in a rather uniform rate being determined by the cis/trans isomerisation of proline peptide bonds.

Keywords

Osteogenesis Imperfecta Triple Helix Globular Domain Correct Alignment Triple Helical Structure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Copyright information

© Springer-Verlag Berlin Heidelberg 1989

Authors and Affiliations

  • R. Dölz
    • 1
  • J. Engel
    • 1
  • K. Kühn
    • 2
  1. 1.BiocenterBaselSwitzerland
  2. 2.MPIMartinsriedGermany

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