Some observations on the fine structure of elastoidin

Electron microscopy of positively stained elastoidin reveals a fine structure apparently identical with that of the collagen of rat tail tendon. The negatively stained pattern is clearly related to that of the collagen but differs from it; it resembles that of artificially cross-linked collagens more. X-ray diffraction fails to find evidence of any long range lateral order in the arrangement of molecules within the elastoidin. The interesting splitting of the meridional pattern upon drying is re-reported and its possible origins discussed. Some discussion of fibrillogenesis is presented based on a comparison of rat tail tendon collagen and elastoidin.

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The equivalence of electron-microscope and X-ray observations on collagen fibres

Proceedings of the Royal Society of London Series A - Mathematical and Physical Sciences ◽

10.1098/rspa.1955.0242 ◽

1955 ◽

Vol 233 (1192) ◽

pp. 1-16 ◽

Cited By ~ 18

Keyword(s):

Fine Structure ◽

Electron Microscope ◽

Density Fluctuations ◽

Density Functions ◽

X Ray Diffraction ◽

X Ray ◽

Biological Interest ◽

Wide Range ◽

Tail Tendon ◽

Rat Tail

One of the outstanding properties of collagen fibrils is an axial periodicity of about 640 Å and associated fine structure which can be observed directly in the electron microscope and also may be deduced from observation of low-angle X-ray diffraction. This paper gives first an account of measurements of density fluctuations along the fibril axis for unstained, unshadowed fibrils for one mammalian collagen, rat-tail tendon, and one avian collagen, fowl-neck tendon. The main and subsequent part of the paper shows how the density functions derived from electron micrographs obtained under specified conditions may be used to calculate the intensities of low-angle X-ray diffraction. Complications arise from the fact—of considerable biological interest—that for any one material a wide range of fine structure exists. For this reason it has been necessary to introduce a modulating function to represent the behaviour of a system of fibrils with differing density functions. The calculated structure amplitudes are compared with those measured from low-angle X-ray photographs of dry fibres. Good agreement between the two sets of results is found for rat-tail tendon and fair agreement for fowl-neck tendon. The agreement for fowl-neck tendon is improved by the application of a more general modulating function.

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Struktur und mechanische Eigenschaften dermatosparaktischen Kollagens / Structure and Mechanical Properties of Dermatosparactic Collagen

Zeitschrift für Naturforschung C ◽

10.1515/znc-1977-9-1013 ◽

1977 ◽

Vol 32 (9-10) ◽

pp. 743-747 ◽

Cited By ~ 4

Author(s):

R. Jonak ◽

Ch. M. Lapière ◽

A. Meinel ◽

H. Nemetschek-Gansler ◽

Th. Nemetschek ◽

...

Keyword(s):

Electron Microscopy ◽

Mechanical Properties ◽

Tensile Strength ◽

Cyclic Extension ◽

X Ray Diffraction ◽

Mechanische Eigenschaften ◽

X Ray ◽

Mechanical Measurements ◽

Tail Tendon ◽

Tendon Collagen

Abstract Dermatosparactic calf-tail-tendon-collagen was investigated by mechanical measurements, electron microscopy and x-ray diffraction. We suppose, that the tensile strength decrease of the fibres is due to the irregular aggregation of subfibrils to fibrils. The x-ray diagram of the fibre is not influenced by state of disorder. Cyclic extension of dermatosparactic collagen leads to a higher increase in tensile strength than in the case of normal calf tendon. The effect might be due to the increase of fibril-and area-density resulting in an augmentation of crosslinks.

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X-ray diffraction effects related to superstructure in rat tail tendon collagen

Biochimica et Biophysica Acta (BBA) - Protein Structure ◽

10.1016/0005-2795(78)90092-2 ◽

1978 ◽

Vol 535 (2) ◽

pp. 253-271 ◽

Cited By ~ 14

Author(s):

L.J. Gathercole ◽

A. Keller

Keyword(s):

X Ray Diffraction ◽

X Ray ◽

Tail Tendon ◽

Diffraction Effects ◽

Rat Tail ◽

Tendon Collagen

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X-ray diffraction of rat tail tendon at ambient and cryo-cooled temperatures - a comparison

Fibre Diffraction Review ◽

10.1382/s200311119 ◽

2003 ◽

Vol 11 (11) ◽

pp. 119

Author(s):

J. H. Laing ◽

J.P.R.O. Orgel ◽

J. Dubochet ◽

A. Al-Amoudi ◽

T. J. Wess ◽

...

Keyword(s):

X Ray Diffraction ◽

X Ray ◽

Tail Tendon ◽

Rat Tail

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Studies on Hierarchical Structures, Formation Mechanism and Functional Properties of Collagen Fibrils. IV. Structure Analysis on Collagen Fibril in Rat Tail Tendon Based on the Small-Angle X-ray-Diffraction Pattern and Energy Calculation.

Sen i Gakkaishi ◽

10.2115/fiber.52.11_591 ◽

1996 ◽

Vol 52 (11) ◽

pp. 591-597

Author(s):

Takashi Itoh ◽

Yutaka Takahashi ◽

Hajime Tsuchiya ◽

Masato Hashimoto ◽

Takashi Konishi

Keyword(s):

Diffraction Pattern ◽

Structure Analysis ◽

Small Angle ◽

Collagen Fibril ◽

Hierarchical Structures ◽

Energy Calculation ◽

X Ray Diffraction ◽

X Ray ◽

Tail Tendon ◽

Rat Tail

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Effect of covalent cross-linking on the X-ray diffraction properties of chick bone and rat tail tendon collagens

Archives of Biochemistry and Biophysics ◽

10.1016/0003-9861(69)90237-9 ◽

1969 ◽

Vol 129 (2) ◽

pp. 769-771 ◽

Cited By ~ 12

Author(s):

E.D. Eanes ◽

E.J. Miller

Keyword(s):

Cross Linking ◽

X Ray Diffraction ◽

X Ray ◽

Tail Tendon ◽

Rat Tail

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Differences in the Fibril Structure of Corneal and Tendon Collagen. An Electron Microscopy and X-Ray Diffraction Investigation

Connective Tissue Research ◽

10.3109/03008208609001985 ◽

1986 ◽

Vol 15 (4) ◽

pp. 269-281 ◽

Cited By ~ 38

Author(s):

M. Marchini ◽

M. Morocutti ◽

A. Ruggeri ◽

M. H.J. Koch ◽

A. Bigi ◽

...

Keyword(s):

Electron Microscopy ◽

X Ray Diffraction ◽

X Ray ◽

Fibril Structure ◽

Tendon Collagen

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Binding of Aliphatic Dihydroxy Compounds to Collagen with X-ray Diffraction Evidence for the Vander Waals Bond

Advances in X-ray Analysis ◽

10.1154/s0376030800008430 ◽

1970 ◽

Vol 14 ◽

pp. 268-274

Author(s):

E. H. Shaw

Keyword(s):

Collagen Fiber ◽

Fiber Axis ◽

X Ray Diffraction ◽

Extended Form ◽

Core Diameter ◽

X Ray ◽

The Core ◽

Collagen Lattice ◽

Tail Tendon ◽

Rat Tail

AbstractPrevious work presented by the author at these conferences has been summarized by G.N. Ramachandran in “Treatise on Collagen I , 177-8”. Epitactic crystallization of amides and diols in the collagen lattice of formalinized rat tail tendon, with equatorial expansion of the collagen lattice, was used to visualize the core diameter of each coil in the triple spiral at 7A and the vertical repeat of the hydrogen-bonding unit at 5.2A. Expansion of the non - formalinized collagen lattice has been observed as high as 20.1A when 1, 4-trans-(bisamino-methyl) - cyclo-hexane was inserted between the hexagonal array of protein spirals in the collagen lattice, the length of the inserted molecule being 13A. With dimensions based on Fisher - Hirschfelder - Taylor atomic models, with maximum extension of the dihydroxy compounds, the a. parameter of the expanded collagen would be expected to increase from 16.5A in the case of glycol to 20.6A in the case of 1, 5 - pentanediol, but actually the parameter decreases from 18.3A in the case of glycol to 16.2A in the case of 1, 5 - pentanediol. The larger figure in the case of glycol is explained by its hydrogen bonded dimerization. 1,3 propanediol fits in to the collagen lattice as its extended form. In the case of the other compounds, the chains are folded and fit together with Vander Waals bonding, and produce progressively smaller parameters for the a axis in collagen. In this nonaqueous equilibrium the non - formalinized collagen core diameter averages 7.7A ±0.2 and the spacing of hydrogen bond contacts along the collagen fiber axis is 4.8 ±0.2A.

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