Applied Biochemistry and Biotechnology

, Volume 69, Issue 2, pp 91–97

Observation of geometric structure of collagen molecules by atomic force microscopy

  • V. Baranauskas
  • B. C. Vidal
  • N. A. Parizotto
Original Articles

DOI: 10.1007/BF02919391

Cite this article as:
Baranauskas, V., Vidal, B.C. & Parizotto, N.A. Appl Biochem Biotechnol (1998) 69: 91. doi:10.1007/BF02919391


Atomic force microscopy was used to study the geometric structure of collagen fibrils and molecules of rat calcanean tendon tissues. The authors found that the diameter of the fibrils ranged from 124 to 170 nm, and their geometric form suggested a helical winding with spectral period from 59.4 to 61.7 nm, close to the band dimensions reported by electron microscopy. At high magnification, the surface of these bands revealed images that probably correspond to the almost crystalline array of collagen molecules, with the triple helix structure almost visible. The typical helix width is 1.43 nm, with main periods of 1.15 and 8.03 nm, very close to the dimensions reported by X-ray diffraction.

Index Entries

Atomic force microscopy collagen molecules collagen fibrils rat tendon 

Copyright information

© Humana Press Inc. 1998

Authors and Affiliations

  • V. Baranauskas
    • 1
  • B. C. Vidal
    • 2
  • N. A. Parizotto
    • 3
  1. 1.Department of Semiconductors and Photonics
  2. 2.Department of Cell Biology, C. P. 6109State University of CampinasCampinasBrazil
  3. 3.Physiotherapy DepartmentUniversidade Federal de São CarlosBrazil

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