The structure of collagen

A. Miller, J. Bradshaw, E. Y. Jones, R. D. Fraser, T. P. MacRae, E. Suzuki

Research output: Contribution to journalArticlepeer-review


A knowledge of the structure of collagen fibrils is important for any rational discussion of the occurrence and treatment of fibrosis. The different genetic types of collagen, and the structure of the triple-helical molecule as refined from X-ray fibre diffraction data, are described. The problem of determining molecular arrangement in native tissues is discussed. The various models proposed for the molecular arrangement of type I collagen are compared and an account is given of the quasi-hexagonal model. A detailed analysis of the X-ray diffraction patterns from native type I collagen fibres is used to provide a quantitative description of the quasi-hexagonal model. Parameters such as molecular positions, azimuthal orientation and axial shift can be estimated from the diffraction patterns. These parameters refer to the helix main-chain. Side-chain conformations can then be built in by molecular graphics and the predicted X-ray pattern for the complete model compared with the observed pattern.

Original languageEnglish
Pages (from-to)65-79
Number of pages15
JournalCiba Foundation symposium
Publication statusPublished - 1 Jan 1985

ASJC Scopus subject areas

  • General


Dive into the research topics of 'The structure of collagen'. Together they form a unique fingerprint.

Cite this