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  • 1
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    Silk properties determined by gland-specific expression of a spider fibroin gene family (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: Spiders produce a variety of silks that range from Lycra-like elastic fibers to Kevlar-like superfibers. A gene family from the spider Araneus diadematus was found to encode silk-forming proteins (fibroins) with different proportions of amorphous glycine-rich domains and crystal domains built from poly(alanine) and poly(glycine-alanine) repeat motifs. Spiders produce silks of different composition by gland-specific expression of this gene family, which allows for a range of mechanical properties according to the crystal-forming potential of the constituent fibroins. These principles of fiber property control may be important in the development of genetically engineered structural proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guerette, P A -- Ginzinger, D G -- Weber, B H -- Gosline, J M -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of British Columbia, Vancouver, British Columbia, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600519" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Animals ; Base Sequence ; Blotting, Northern ; Crystallization ; DNA, Complementary/genetics ; Exocrine Glands/*metabolism ; Fibroins/*chemistry/genetics ; Gene Expression Regulation ; Gene Library ; *Insect Proteins ; Molecular Sequence Data ; Peptides/analysis ; Proline/analysis ; Protein Structure, Secondary ; Proteins/chemistry/genetics ; *Silk ; Spiders/*chemistry/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Elastic arteries in invertebrates: mechanics of the octopus aorta (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-14
    Description: The aorta of the octopus, Octopus dofleini, is a highly distensible, elastic tube. The circumferential elastic modulus increases with inflation in the physiological range from abut 10(4) to 10(5) newtons per square meter. Rubber-like fibers have been isolated, apparently for the first time, from the aorta of an invertebrate. These fibers have an elastic modulus, like elastin, of about 4 x 10(5) newtons per square meter and are present in sufficient quantity to account for the elastic properties of the intact vessel under physiological conditions. Thus the circulatory system of an invertebrate animal provides an "elastic reservoir" (much like that of the vertebrate system), which increases the efficiency of the circulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shadwick, R E -- Gosline, J M -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):759-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256277" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta/anatomy & histology/*physiology ; Elasticity ; Octopodiformes/*physiology ; Proteins/physiology ; Species Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
    Electronic Resource
    Electronic Resource
    Optical properties of single elastin fibres indicate random protein conformation (1980)
    [s.l.] : Nature Publishing Group
    Nature 287 (1980), S. 865-867 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Polarized light microscopy is a useful technique because unlike electron microscopy it does not require any physical modification of the protein structure, and thus it reduces the chance of procedural artefacts. Further, the technique allows the evaluation of structure at two levels of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/287865a0
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  • 4
    Electronic Resource
    Electronic Resource
    Elastin as a random-network elastomer: A mechanical and optical analysis of single elastin fibers (1981)
    New York : Wiley-Blackwell
    Biopolymers 20 (1981), S. 1247-1260 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The physical properties of single, 5-8-μm diameter, water-swollen elastin fibers have been investigated on a microtest apparatus attached to a polarizing microscope. Analysis of the mechanical and optical properties at extensions below 100% indicate that the elastic modulus (G) has a value of 4.1 × 105 N m-2, the average molecular weight of chains between crosslinks is in the range of 6000-7100, and the stress optical coefficient (C′) is 1 × 10-9 m2 N-1 at 24°C. Analysis of the temperature dependence of the stress optical coefficient indicates that the polarizability of the random link decreases with increasing temperature, with an apparent activation energy for this process of the order of 1.6 kcal/mol. Analysis of the non-Gaussian mechanical and optical properties at extensions above about 100% suggest that the chains between crosslinks contain approximately 10 “effective” random links, with each link consisting of 7-8 amino acid residues. These parameters for the random chains in the elastin network have been used to predict the dimensions of other random proteins. The close correlation of these predictions with published values for the dimensions of a series of proteins in solution in 6M guanidinium hydrochloride provides an independent test of the appropriateness of our analysis.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1981.360200611
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  • 5
    Electronic Resource
    Electronic Resource
    The effects of hydration on the dynamic mechanical properties of elastin (1990)
    New York : Wiley-Blackwell
    Biopolymers 29 (1990), S. 1147-1160 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The dynamic mechanical properties of elastin have been quantified over a temperature and hydration range appropriate for a biological polymer. Composite curves of the tensile properties at constant water contents between 28.1 and 44.6% (g water/100 g protein) were typical of an amorphous polymer going through its glass transition. Water content had no effect on the shape of the curves, but shifted them a distance aC along the frequency axis. The combined effects of hydration and temperature are given in a series of isoshift curves where elastin's properties are constant along any one curve. A 1% change in hydration has the same effect as a 1°-2° change in temperature, depending on the initial water content and temperature. Theoretical isoshift curves that matched the experimental data were predicted using the WLF equation and coefficients determined from the data. These data form a basis to predict the role of elastin in arterial disease based on changes in its chemical and physical environment.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360290805
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  • 6
    Electronic Resource
    Electronic Resource
    Elastin dehydration through the liquid and the vapor phase: A comparison of osmotic stress models (1996)
    New York : Wiley-Blackwell
    Biopolymers 39 (1996), S. 627-639 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The swelling and viscoelastic behaviors of samples of purified arterial elastin were investigated to develop a model for studying the viscoelastic behavior of elastin. Two osmotic stress models were used: the vapor phase model (VPM), in which the stress on the elastin sample was applied through the vapor phase by equilibrating the sample over a saline solution, and the liquid phase model (LPM), in which the stress was applied through the liquid phase by equilibrating the sample in aqueous solutions of large molecular weight polymers. The elastin in the VPM showed a highly varied viscoelastic response, and was slightly stiffer and had a slightly higher damping coefficient than the elastin in the LPM at equivalent nominal relative humidities. We believe the difference in behavior of the elastin in the two models was due to geometric distortions of the elastin that occur during dehydration in the VPM. In the LPM, the spaces between the elastin fibrils are filled with water, and in the VPM these spaces collapse when the water is removed. Removal of only the interfibrillar water deswelled the tissue and increased its stiffness and damping coefficient.Viscoelastic spectra obtained at different levels of osmotic stress in the LPM were reducible to one master curve, indicating that the dominant effect of dehydration is a nonspecific reduction of molecular mobility. We conclude that the LPM is a better model than the VPM for studying the effects of dehydration on the mechanical behavior of elastin. © 1996 John Wiley & Sons, Inc.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Swelling and viscoelastic properties of osmotically stressed elastin (1996)
    New York : Wiley-Blackwell
    Biopolymers 39 (1996), S. 641-652 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The swelling and viscoelastic properties of purified elastin were studied in aqueous solutions of superswelling agents or osmotic deswelling agents to develop models to study the behavior of elastin at frequencies not easily accessible by direct measurement. Increasing the concentration of any of the deswelling solutes (glucose, sucrose, sodium chloride, ammonium sulphate, dextran, and polyethylene glycol) increased the tensile storage and loss moduli. The viscoelastic behavior was independent of solute when compared on the basis of swelling behavior. The data collected at various solute concentrations at 37°C could be reduced to one master curve, and the master curves for elastin in each of the deswelling solutes were themselves superposable. The ability to reduce the data indicates that dehydration can be used to model elastin's viscoelastic behavior at high frequencies or over short times.The viscoelastic behavior of elastin in the superswelling agents [potassium thiocyanate (KSCN), dimethyl sulfoxide (DMSO), and ethylene glycol (EG)] depended on the solute and was independent of swelling behavior. In KSCN the behavior of elastin seemed to be a continuation of the pattern established by the deswelling agents in that an increase in swelling was accompanied by a decrease in both moduli, and the viscoelastic spectra were reducible to one master curve. In high concentrations of DMSO and EG the spectra were not reducible. KSCN appears a suitable superswelling solute to model elastin's viscoelastic behavior at low frequencies or over long times. © 1996 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
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  • 8
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    Optical properties of single elastin fibres indicate random protein conformation (1980)
    Springer Nature
    Details
    Publication Date: 1980-10-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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