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Comparisons of Recombinant Resilin-like Proteins: Repetitive Domains Are Sufficient to Confer Resilin-like Properties

Biomacromolecules, 2009
Two novel recombinant proteins An16 and Dros16 have recently been generated. These recombinant proteins contain, respectively, sixteen copies of an 11 amino acid repetitive domain (AQTPSSQYGAP) observed in a resilin-like gene from Anopheles gambiae and sixteen copies of a 15 amino acid repetitive domain (GGRPSDSYGAPGGGN) observed in the first exon of ...
Lyons, RE   +5 more
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Recombinant Resilin—A Protein-Based Elastomer

2008
Elastomeric proteins are a diverse group of structural proteins present in widely divergent organisms from insects and mollusks to higher mammals. They are structural proteins displaying reversible deformation and serve an important functional role in providing long-range elasticity, storing kinetic energy, acting as shock absorbers and as antagonists ...
Huson, Mickey G., Elvin, Christopher M.
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Relations of various collagens, elastin, resilin and fibroin

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972
Abstract 1. 1. The fibrous and membranous types of collagens have a common origin. Similar development has occurred in both collagens with regard to the amino acid composition to increase the heat stability. 2. 2. During the evolution of fibrous collagen the amino acids with short side chains have increased to facilitate a close packing. 3.
J, Pikkarainen, E, Kulonen
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Bioinspired High Resilient Elastomers to Mimic Resilin

ACS Macro Letters, 2016
Natural resilin possesses outstanding mechanical properties, such as high strain, low stiffness, and high resilience, which are difficult to be reproduced in synthetic materials. We designed high resilient elastomers (HREs) with a network structure to mimic natural resilin on the basis of two natural abundant polymers, stiff cellulose and flexible ...
Zhongkai, Wang   +5 more
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Tentative identification of a resilin gene in Drosophila melanogaster

Insect Biochemistry and Molecular Biology, 2001
A search of the Drosophila genome for gene products with similarities to the amino acid sequences of three tryptic peptides from locust (Schistocerca gregaria) resilin gave two positive results: gene products CG15920 and CG9036. In both conceptual translation products a 62-residue region is present, which is identical to the resilin peptides in 29 ...
Ardell, David H., Andersen, Svend Olav
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Properties of Resilin, a Rubberlike Protein

Rubber Chemistry and Technology, 1963
Abstract There is much circumstantial evidence in favor of the belief that elastin and some other structural proteins exist in the rubberlike state of matter (see reviews by Wöhlisch, 1939; Astbury, 1940; Meyer, 1950; Kendrew, 1954), but it will be shown that the crucial evidence from thermodynamic experiments is ambiguous.
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Factors affecting the tertiary structure of resilin in locusts

Journal of Cell Science, 1967
ABSTRACT Autofluorescent daily growth zones in locust resilin provide a detailed record of cross-linking of the polypeptide chains, since the fluorescence is caused by the tertiary cross-links, dityrosine and trityrosine. Environmental temperature changes are the main cause of autofluorescent daily growth layers in resilin, fluorescence ...
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Function of Resilin in Tsetse Fly Feeding Mechanism

Nature, 1970
RESILIN is an elastic structural protein which was discovered by Weis-Fogh in the wing-hinges of locusts1. The substance can be identified with certainty only by the use of several tests, by means of which it has been demonstrated in specific areas of cuticle in insects and crustacea2.
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Resilin

2008
Norman C. Leppla   +33 more
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