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Oriented Crystallization of Amides on Collagen with Modification of the Collagen Lattice

Published online by Cambridge University Press:  06 March 2019

E. H. Shaw Jr.
E. H. Shaw Jr.*
Affiliation:
University of South Dakota Vermillion, South Dakota
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Abstract

Rat tail tendons were fixed in 4% formaldehyde at 250 g tension, soaked in nearly saturated solution of the amides involved, and dried while still under tension. X-ray diffraction patterns, taken with rotation around the collagen fiber axis, showed well-defined layer lines of the amide and usually substantial expansion of the collagen equatorial spacing.

The layer lines on collagen, in two cases on abnormal or polymorphic axes, are clustered around the number 4.86 ± 0.33 Å, or a figure twice this, implying the presence of a repeating hydro gen-bond accepting group such as the carbonyl group at this interval. The prominent collagen layer line at 9.4 Å is approximately double this interval.

Type
Research Article
Information
Advances in X-Ray Analysis , Volume 7: Twelfth Annual Conference on Applications of X-ray Analysis, August 7-9, 1963 , 1963 , pp. 252 - 255
Copyright
Copyright © International Centre for Diffraction Data 1963

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