Literature DB >> 9513990

Observation of geometric structure of collagen molecules by atomic force microscopy.

V Baranauskas1, B C Vidal, N A Parizotto.   

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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Year:  1998        PMID: 9513990     DOI: 10.1007/bf02919391

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  3 in total

1.  Ultrastructural localisation and size distribution of collagen fibrils in Glisson's sheath of rat liver: implications for mechanical environment and possible producing cells.

Authors:  Y Hosoyamada; H Kurihara; T Sakai
Journal:  J Anat       Date:  2000-04       Impact factor: 2.610

2.  LLLT improves tendon healing through increase of MMP activity and collagen synthesis.

Authors:  Flávia Da Ré Guerra; Cristiano Pedrozo Vieira; Marcos Santos Almeida; Letícia Prado Oliveira; Andrea Aparecida de Aro; Edson Rosa Pimentel
Journal:  Lasers Med Sci       Date:  2012-11-21       Impact factor: 3.161

3.  Topographic changes in SARS coronavirus-infected cells at late stages of infection.

Authors:  M L Ng; J W M Lee; M L N Leong; A-E Ling; H-C Tan; E E Ooi
Journal:  Emerg Infect Dis       Date:  2004-11       Impact factor: 6.883

  3 in total

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