Observation of geometric structure of collagen molecules by atomic force microscopy

被引:28
作者
Baranauskas, V
Vidal, BC
Parizotto, NA
机构
[1] Univ Estadual Campinas, Dept Semicond & Photon, BR-13083 Campinas, SP, Brazil
[2] Univ Estadual Campinas, Dept Cell Biol, BR-13083 Campinas, SP, Brazil
[3] Univ Fed Sao Carlos, Dept Physiotherapy, BR-13560 Sao Carlos, SP, Brazil
基金
巴西圣保罗研究基金会;
关键词
atomic force microscopy; collagen molecules; collagen fibrils; rat tendon;
D O I
10.1007/BF02919391
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:91 / 97
页数:7
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