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Molecular tilting in dried elastoidin and its implications for the structures of other collagen fibrils.

Abstract：

:Wet elastoidin spicules (fish fin rays) yield low-angle meridional X-ray diffraction patterns which resemble those from tendons. However, when the spicule dries the meridian splits into the arms of a diagonal cross (sometimes only one arm appears). Of the possible explanations we reject shearing of the axial arrangement of molecules but confirm tilting. We suggest that, in three dimensions, the molecules are tilted at angles which vary from 0 degrees at the centre to some maximum value at the surface of the spicule, resembling torsion of the array of molecules. Molecular tilting probably occurs in other collagen fibrils.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Hukins DW,Woodhead-Galloway J,Knight DP

doi

10.1016/0006-291x(76)90229-1

subject

Has Abstract

pub_date

1976-12-20 00:00:00

pages

1049-55

issue

4

eissn

0006-291X

issn

1090-2104

pii

0006-291X(76)90229-1

journal_volume

73

pub_type

杂志文章

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