title: Crimp as part of a helical structure.
abstract: Crimp is generally conceived of as a ribbon, i.e. a planar periodic orientation variation of collagen fibers. This study was carried out to demonstrate that crimps are complex structures with the possibility of being helically arranged. Thick sections, imbibed in glycerol or even in mineral oil and studied under the polarizing microscope with the help of 1st order red and lambda/4 Sénarmont's compensators proved to be adequate to detect details of collagen fiber orientation with respect to crimp structure. It was found that collagen bundles are ordered aggregates forming helical structures, and crimps are part of such a helical arrangement. The major part of the macromolecules in tendons have a helix conformation that probably influences a complex hierarchical construct. It is possible that thermodinamically this ordering is better fitted to respond to the biomechanical requirements of the tendons and to correspond to their rheological properties.
authors.affiliation: Departamento de Biologia Celular, IB, CP. 6109 UNICAMP, SP, Brazil.
authors.forename: B de C
authors.initials: Bde C
authors.lastname: Vidal
mesh_terms: D000818:Animals; D002417:Cattle; D003094:Collagen; D008297:Male; D008859:Microscopy, Polarization; D051381:Rats; D013710:Tendons / Q000648:ultrastructure*
chemical_list: D003094:Collagen