Author: Habelitz S. Balooch M. Marshall S.J. Balooch G. Marshall G.W.
Publisher: Academic Press
ISSN: 1047-8477
Source: Journal of Structural Biology, Vol.138, Iss.3, 2002-06, pp. : 227-236
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Abstract
Dentin collagen fibrils were studied in situ by atomic force microscopy (AFM). New data on size distribution and the axial repeat distance of hydrated and dehydrated collagen type I fibrils are presented. Polished dentin disks from third molars were partially demineralized with citric acid, leaving proteins and the collagen matrix. At this stage collagen fibrils were not resolved by AFM, but after exposure to
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