Abstract：
:In order to understand whole tooth behavior under load the biomechanical role of enamel and dentin has to be determined. We approach this question by comparing the deformation pattern and stiffness of intact teeth under load with the deformation pattern and stiffness of the same teeth after the enamel has been mechanically compromised by introducing a defect. FE models of intact human premolars, based on high resolution micro-CT scans, were generated and validated by in vitro electronic speckle pattern interferometry (ESPI) experiments. Once a valid FE model was established, we exploit the flexibility of the FE model to gain more insight into whole tooth function. Results show that the enamel cap is an intrinsically stiff biological structure and its morphology dictates the way a whole tooth will mechanically behave under load. The mechanical properties of the enamel cap were sufficient to mechanically maintain almost its entire stiffness function under load even when a small defect (cavity simulating caries) was introduced into its structure and breached the crown integrity. We conclude that for the most part, that enamel and not dentin dictates the mechanical behavior of the whole tooth.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Barak MM,Geiger S,Chattah NL,Shahar R,Weiner Sdoi
10.1016/j.jsb.2009.07.019subject
Has Abstractpub_date
2009-12-01 00:00:00pages
511-20issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(09)00205-6journal_volume
168pub_type
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journal_title：Journal of structural biology
pub_type： 杂志文章
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journal_title：Journal of structural biology
pub_type： 杂志文章
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
pub_type： 杂志文章
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pub_type： 杂志文章
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pub_type： 杂志文章
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journal_title：Journal of structural biology
pub_type： 杂志文章
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更新日期：2010-01-01 00:00:00
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pub_type： 杂志文章
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journal_title：Journal of structural biology
pub_type： 杂志文章
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更新日期：2015-08-01 00:00:00
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journal_title：Journal of structural biology
pub_type： 杂志文章
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更新日期：2016-06-01 00:00:00
abstract：:Cryogenic electron microscopy (cryo-EM) and single-particle analysis enables determination of near-atomic resolution structures of biological molecules. However, large computational requirements limit throughput and rapid testing of new image processing tools. We developed PRIME, an algorithm part of the SIMPLE softwa...
journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2018.08.005
更新日期：2018-11-01 00:00:00
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journal_title：Journal of structural biology
pub_type： 杂志文章,评审
doi：10.1006/jsbi.2000.4289
更新日期：2000-06-01 00:00:00
abstract：:Human scalp hairs are often examined microscopically to study the variation and diversity among a range of visible morphological traits. In this study, we focused on the ultrastructure of human scalp hair within its keratinized matrix, emphasizing, the density and distribution of melanosomes, variation in cuticle thic...
journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1016/j.jsb.2018.11.008
更新日期：2019-01-01 00:00:00
abstract：:Traditional single particle reconstruction methods use either the Fourier or the delta function basis to represent the particle density map. This paper proposes a more flexible algorithm that adaptively chooses the basis based on the data. Because the basis adapts to the data, the reconstruction resolution and signal-...
journal_title：Journal of structural biology
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doi：10.1016/j.jsb.2012.04.012
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abstract：:Hitherto, the packing arrangement of the aquaporin-1 (AQP1) tetramer in 2-dimensional (2-D) crystals (two-sided plane group p42(1)2) was observed to be largely similar (canonical crystal form) despite the difference in the source of the protein, the glycosylation state of the protein, the type of lipids, and the ratio...
journal_title：Journal of structural biology
pub_type： 杂志文章
doi：10.1006/jsbi.2000.4211
更新日期：2000-05-01 00:00:00
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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更新日期：2019-11-01 00:00:00
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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abstract：:Human coagulation factor VIIai that lacks the Gla domain (residues 1-44) has been prepared, purified, and crystallised. First, recombinant factor VII was activated to form factor VIIa, the active site was then inhibited with 1,5-dansyl-Glu-Gly-Arg-chloromethyl ketone, and finally the Gla domain was removed by chymotry...
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