Observation of geometric structure of collagen molecules by atomic force microscopy |
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Authors: | V. Baranauskas B. C. Vidal N. A. Parizotto |
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Affiliation: | 1. Department of Semiconductors and Photonics, Av. Albert Einstein, N.400 2. Department of Cell Biology, C. P. 6109, State University of Campinas, P. O. Box 6101, 13083, Campinas, SP, Brazil 3. Physiotherapy Department, Universidade Federal de S?o Carlos, 13560, S?o Carlos, Brazil
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Abstract: | 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. |
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Keywords: | KeywordHeading" >Index Entries Atomic force microscopy collagen molecules collagen fibrils rat tendon |
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