dc.creatorBaranauskas, V
dc.creatorVidal, BC
dc.creatorParizotto, NA
dc.date1998
dc.dateFEB
dc.date2014-12-02T16:24:56Z
dc.date2015-11-26T17:20:15Z
dc.date2014-12-02T16:24:56Z
dc.date2015-11-26T17:20:15Z
dc.date.accessioned2018-03-29T00:07:52Z
dc.date.available2018-03-29T00:07:52Z
dc.identifierApplied Biochemistry And Biotechnology. Humana Press Inc, v. 69, n. 2, n. 91, n. 97, 1998.
dc.identifier0273-2289
dc.identifierWOS:000072337200002
dc.identifier10.1007/BF02919391
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/62312
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/62312
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/62312
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1283090
dc.descriptionAtomic force microscopy was used to study the geometric structure of collagen fibrils and molecules of rat calcanean tendon tissues. The authors found that the diameter of the fibrils ranged from 124 to 170 nm, and their geometric form suggested a helical winding with spectral period from 59.4 to 61.7 nm, close to the band dimensions reported by electron microscopy. At high magnification, the surface of these bands revealed images that probably correspond to the almost crystalline array of collagen molecules, with the triple helix structure almost visible. The typical helix width is 1.43 nm, with main periods of 1.15 and 8.03 nm, very close to the dimensions reported by X-ray diffraction.
dc.description69
dc.description2
dc.description91
dc.description97
dc.languageen
dc.publisherHumana Press Inc
dc.publisherTotowa
dc.publisherEUA
dc.relationApplied Biochemistry And Biotechnology
dc.relationAppl. Biochem. Biotechnol.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectatomic force microscopy
dc.subjectcollagen molecules
dc.subjectcollagen fibrils
dc.subjectrat tendon
dc.subjectPacking
dc.subjectFibrils
dc.subjectModel
dc.titleObservation of geometric structure of collagen molecules by atomic force microscopy
dc.typeArtículos de revistas


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