1974
DOI: 10.1007/bf01387962
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Dynamic mechanical loss in keratin at low temperatures

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Cited by 27 publications
(5 citation statements)
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References 16 publications
(9 reference statements)
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“…The strain limit of covalent bond stretching (after that molecular fracture occurs) in a single tropocollagen molecule is 0.5 [35]. This is consistent with macroscopic tensile stress-strain measurements on protein tissues such as horn (mainly keratin), tendon and ligament (mainly collagen), where the tensile strain limit is usually 0.5 or less [36][37][38]. The above calculated values are much higher than this elastic limit of 0.5.…”
Section: Non-linear Extension Of Protein Layerssupporting
confidence: 86%
“…The strain limit of covalent bond stretching (after that molecular fracture occurs) in a single tropocollagen molecule is 0.5 [35]. This is consistent with macroscopic tensile stress-strain measurements on protein tissues such as horn (mainly keratin), tendon and ligament (mainly collagen), where the tensile strain limit is usually 0.5 or less [36][37][38]. The above calculated values are much higher than this elastic limit of 0.5.…”
Section: Non-linear Extension Of Protein Layerssupporting
confidence: 86%
“…The dynamic mechanical properties of a-keratin have been investigated in human stratum corneum [30], horse hair [31], and wool [14]. There is a strong correlation between the humidity/water content and the viscoelastic property values.…”
Section: Resultsmentioning
confidence: 98%
“…An up to 10µm long zone means that multiple crystallite nanofibers or even multiple enamel rods are included in the inelastic process and the bridging stress is not only caused by protein bridging alone. Experimental studies showed that the ultimate stress of proteins such as ligaments (mainly collagen), tendon (mainly collagen) and horn (mainly keratin) are 2.5-7MPa, 70MPa and 260MPa respectively (Sikoryn and Hukins, 1990;Bigliana et al, 1992, Meyers et al, 2008Druhala and Feughelman, 1974) and are generally lower than the calculated 163-770MPa Secondly, the stress intensity shielding contributed by the protein bridging can be estimated by using a Dugdale-zone model, K p =2*σ p *f p *(2*l p /π) 0.5 with K p the stress intensity due to protein bridging, σ p =2.5-260MPa the yield strength of protein, f p =0.1 the area fraction of protein bridging ligaments (estimated based on the volume fraction of protein in enamel), l p =1-10µm the protein bridging zone length (Evans and McMeeking, 1986). K p is calculated as 0-0.13MPa.m 0.5 and is much smaller than the crack tip toughness.…”
Section: Discussionmentioning
confidence: 99%