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Cross Linking of Collagen by Hydrophobe Bonds

Published online by Cambridge University Press:  06 March 2019

Edwin H. Shaw Jr.*
Affiliation:
The University of South Dakota Vermillion, South Dakota 57069
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Abstract

Previous work on modification of the collagen lattice, presented at these meetings, has served to confirm the Ramachandran proposal for the structure of this important protein, together with information on the lengths and tensile strengths of these bonds, including hydrogen bonds, hydrophobe bonds, and Vander Waals attractions. Rat tail tendons were suspended in 2 M aqueous solutions of dimethylsulfoxide, acetone, trimethylamineoxide and 1,4-cyclohexanedione, all of which showed evidence of ligation by expansion of the collagen lattice and refinement of the 100 spot in the x-ray diffraction pattern run by rotation on the collagen fiber axis. In the case of trimethylamineoxide and cyclohexanedione, oriented crystallization also occurred, with the long direction of the molecule in the plane perpendicular to the fiber axis of collagen. With the monofunctional ligands, the -C=0 group forms a hydrogen bond to the N-H group in the Ramachandran standard revised model, leaving the methyl groups to form the hydrophobe bond.

Type
Research Article
Copyright
Copyright © International Centre for Diffraction Data 1971

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References

1. Shaw, E. H. Jr., “Oriented Crystallization of Amides on Collagen with Modification of the Collagen Lattice”, in Mueller, W. M., Mallett, G. R., and Fay, M. J., Editors, Advances in X-ray Analysis, Vol. 7, pp. 252-5, Plenum Press (1964).Google Scholar
2. Shaw, E. H. Jr. and Christensen, Alton R., “Modification of Collagen and Nylon Lattices by Resorcinol”, in Mueller, W. M., Mallett, G. R., and Fay, M. J., Editors, Advances in X-ray Analysis, Vol. 8, pp. 175179, Plenum Press (1965).Google Scholar
3. Shaw, E. H. Jr., as quoted by Ramachandran, G. N., “Treatise on Collagen, Vol. I, Chemistry of Collagen”, Academic Press, N.Y., 1967, pp. 177-8.Google Scholar
4. Shaw, E. H. Jr., “Binding of Aliphatic Dihydroxy Compounds to Collagen with X-ray Diffraction Evidence for the Vander Waals Bond”, in Barrett, Charles S., Newkirk, John B., and Ruud, Clayton O., Editors, Advances in X-ray Analysis, Vol. 14, pp. 268274, Plenum Press (1971).Google Scholar
5. Ramachandran, G. N. and Sasisekharan, V., “Refinement of the Structure of Collagen”, Biochim. Biophys. Acta, 109, 314 (1965).Google Scholar