Skip to main content
. Author manuscript; available in PMC: 2016 Apr 11.
Published in final edited form as: Curr Opin Cell Biol. 2007 Oct 17;19(5):578–583. doi: 10.1016/j.ceb.2007.09.005

Figure 1.

Figure 1

Supramolecular organization of collagen fibrils. (a) The superhelical twist of individual fibrillar elements can be seen in this atomic force microscopy image of a mechanically disrupted collagen fibril (ref. [51], reprinted with permission of Wiley-Liss, Inc., a subsidiary of John Wiley & Sons, Inc. Copyright Wiley-Liss, 2006). The box size is 5 μm × 5 μm and the inset height scale corresponds to 0-30 nm. (b-c) Cross-section model of molecular packing in collagen fibrils (adapted with permission from ref. [19]. Copyright Elsevier, 2002). Thousands of individual collagen triple-helices interact to form a single fibril with both ordered and disordered packing features. Collagen microfibrils are formed by five collagen molecules in a staggered arrangement, shown connected by trapezoids in (c).