Observation of geometric structure of collagen molecules by atomic force microscopy

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.

[1]  D. Eyre,et al.  Collagen: molecular diversity in the body's protein scaffold , 1980, Science.

[2]  V Baranauskas,et al.  Observation of baker’s yeast strains used in biotransformation by atomic force microscopy , 1996, Applied biochemistry and biotechnology.

[3]  A. Kajava Molecular packing in type I collagen fibrils. A model with neighbouring collagen molecules aligned in axial register. , 1991, Journal of molecular biology.

[4]  B. Tillmann,et al.  SEM studies of the collagen architecture of the human lamina cribrosa: normal and pathological findings. , 1996, Ophthalmologica. Journal international d'ophtalmologie. International journal of ophthalmology. Zeitschrift fur Augenheilkunde.

[5]  B. Brodsky,et al.  The triple‐lielix motif in proteins , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[6]  Vitor Baranauskas,et al.  Characterization of photodeposited selenium planar structures by scanning force microscopy , 1995 .

[7]  D J Prockop,et al.  Radial packing, order, and disorder in collagen fibrils. , 1995, Biophysical journal.

[8]  T. Ushiki,et al.  Three-dimensional arrangement of collagen and elastin fibers in the human urinary bladder: a scanning electron microscopic study. , 1995, The Journal of urology.

[9]  K. Mayo,et al.  NMR and x-ray studies of collagen model peptides. , 1996, Biopolymers.

[10]  C. Levene Book Review: Treatise on Collagen , 1969 .

[11]  M. Raspanti,et al.  Collagen fibril patterns in compact bone: preliminary ultrastructural observations. , 1996, Acta Anatomica.

[12]  H M Berman,et al.  Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. , 1994, Science.