Collagen fibrillar structure in mineralized and nonmineralized tissues

Arthur Veis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


The four most important recent developments have been the following determinations: first, that collagen molecules have considerable flexibility so that in regions devoid of glycine - proline - proline or glycine - proline - hydroxyproline in each chain, substantial helix distortion can be allowed; second, that this flexibility is reflected by considerable azimuthal disorder in radially-packed fibrils, with the azimuthal order specified, principally, in the cross-linked overlap zones; third, that mineral crystal size and order are tightly linked to the perfection of the collagen packing, although in bone the crystal c-axis may be tilted by as much as ±20° from the fibril axis; and fourth, that the process of mineralization may cause rearrangement of the cross-linkages in the collagen overlap zones.

Original languageEnglish (US)
Pages (from-to)370-378
Number of pages9
JournalCurrent Opinion in Solid State and Materials Science
Issue number3
StatePublished - Jan 1 1997


  • Hyp Hydroxyproline
  • O Hydroxyproline

ASJC Scopus subject areas

  • Materials Science(all)


Dive into the research topics of 'Collagen fibrillar structure in mineralized and nonmineralized tissues'. Together they form a unique fingerprint.

Cite this