Twisted fibrils are a structural principle in the assembly of interstitial collagens, chordae tendineae included.
X-ray diffraction analysis of connective tissue samples, which contain type I and type III collagen shows that twisted collagen fibrils are a general principle of assembly. The occurrence of twisted fibrils in native wet Chordae tendineae, skin and Aorta is combined with a shorter axial periodicity of about 65 nm. This shorter D period is shown to be directly related to the tilt of the molecules, which have to be curved to build-up twisted fibrils.
Folkhard
W
W
Abteilung für Ultrastrukturforschung, Universität Heidelberg, Bundesrepublik Deutschland.
Christmann
D
D
Geercken
W
W
Knörzer
E
E
Koch
M H
MH
Mosler
E
E
Nemetschek-Gansler
H
H
Nemetschek
T
T
D000328:Adult; D001011:Aorta / Q000032:analysis; D002815:Chordae Tendineae / Q000032:analysis*; D003094:Collagen / Q000032:analysis*; D003238:Connective Tissue / Q000032:analysis*; D005385:Fingers; D006801:Humans; D008875:Middle Aged; D008954:Models, Biological; D012044:Regression Analysis; D012867:Skin / Q000032:analysis; D013710:Tendons / Q000032:analysis; D014961:X-Ray Diffraction
D003094:Collagen