{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T08:12:59Z","timestamp":1768723979516,"version":"3.49.0"},"reference-count":38,"publisher":"The Company of Biologists","issue":"3","license":[{"start":{"date-parts":[[1999,2,1]],"date-time":"1999-02-01T00:00:00Z","timestamp":917827200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1999,2,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>An evolutionary trend towards increasing hydrophobicity of vertebrate arterial elastins suggests that there is an adaptive advantage to higher hydrophobicity. The swelling and dynamic mechanical properties of elastins from several species were measured to test whether hydrophobicity is associated with mechanical performance. Hydrophobicity was quantified according to amino acid composition (HI), and two behaviour-based indices: the Flory\u2013Huggins solvent interaction parameter (\u03c71), and a swelling index relating tissue volumes at 60 and 1 \u00b0C. Swelling index values correlated with \u03c71 and, for most species studied, with HI, suggesting that the different approaches used to quantify hydrophobicity are equally valid. Dynamic mechanical properties were measured both in a closed system, to control the effects of water content, and in an open system, to determine whether the increased swelling of hydrophobic materials at low temperatures offsets the direct stiffening effect of cold. There were no biologically significant differences in mechanical behaviour in either open or closed systems that could be attributed to hydrophobicity. Therefore, although the original function of hydrophobicity in an ancestral elastin may have been to produce molecular mobility, mechanical performance did not drive a subsequent increase in hydrophobicity. Higher hydrophobicities may have arisen to facilitate the manufacture of the elastic fibre.<\/jats:p>","DOI":"10.1242\/jeb.202.3.301","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T05:24:25Z","timestamp":1619328265000},"page":"301-314","source":"Crossref","is-referenced-by-count":29,"title":["The hydrophobicity of vertebrate elastins"],"prefix":"10.1242","volume":"202","author":[{"given":"G. W. G.","family":"Chalmers","sequence":"first","affiliation":[{"name":"University of British Columbia Department of Zoology , , Vancouver, Canada V6T 1Z4"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J. M.","family":"Gosline","sequence":"additional","affiliation":[{"name":"University of British Columbia Department of Zoology , , Vancouver, Canada V6T 1Z4"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. A.","family":"Lillie","sequence":"additional","affiliation":[{"name":"University of British Columbia Department of Zoology , , Vancouver, Canada V6T 1Z4"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[1999,2,1]]},"reference":[{"key":"2024110713315126100_JEXBIO_202_3_301C1","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1038\/287865a0","article-title":"Optical properties of single elastin fibres indicate random protein conformation","volume":"287","author":"Aaron","year":"1980","journal-title":"Nature"},{"key":"2024110713315126100_JEXBIO_202_3_301C2","doi-asserted-by":"publisher","first-page":"1247","DOI":"10.1002\/bip.1981.360200611","article-title":"Elastin as a random-network elastomer: a mechanical and optical analysis of single elastin fibres","volume":"20","author":"Aaron","year":"1981","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C3","first-page":"633","article-title":"Resilin","volume-title":"In Comprehensive Biochemistry","author":"Anderson","year":"1971"},{"key":"2024110713315126100_JEXBIO_202_3_301C4","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1016\/0022-5193(67)90004-5","article-title":"On the average hydrophobicity of proteins and the relation between it and protein structure","volume":"16","author":"Bigelow","year":"1967","journal-title":"J. Theor. Biol"},{"key":"2024110713315126100_JEXBIO_202_3_301C5","doi-asserted-by":"publisher","first-page":"1499","DOI":"10.1021\/ja01237a025","article-title":"Adsorption of water vapor by proteins","volume":"66","author":"Bull","year":"1944","journal-title":"J. Am. Chem. Soc"},{"key":"2024110713315126100_JEXBIO_202_3_301C6","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1016\/S0065-3233(08)60480-5","article-title":"The thermodynamic basis of the stability of proteins, nucleic acids and membranes","volume":"30","author":"Edelhoch","year":"1976","journal-title":"Adv. Protein Chem"},{"key":"2024110713315126100_JEXBIO_202_3_301C7","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1039\/fs9821700109","article-title":"Hydrophobic moments and protein structure","volume":"17","author":"Eisenberg","year":"1982","journal-title":"Faraday Symp. Chem. Soc"},{"key":"2024110713315126100_JEXBIO_202_3_301C8","volume-title":"Viscoelastic Properties of Polymers","author":"Ferry","year":"1970"},{"key":"2024110713315126100_JEXBIO_202_3_301C9","volume-title":"Principles of Polymer Chemistry","author":"Flory","year":"1953"},{"key":"2024110713315126100_JEXBIO_202_3_301C10","doi-asserted-by":"publisher","first-page":"697","DOI":"10.1002\/bip.1978.360170312","article-title":"The temperature-dependent swelling of elastin","volume":"17","author":"Gosline","year":"1978","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C11","doi-asserted-by":"publisher","first-page":"2091","DOI":"10.1002\/bip.1979.360180818","article-title":"Dynamic mechanical properties of elastin","volume":"18","author":"Gosline","year":"1979","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C12","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1126\/science.272.5258.112","article-title":"Silk properties determined by gland-specific expression of a spider fibroin gene family","volume":"272","author":"Guerette","year":"1996","journal-title":"Science"},{"key":"2024110713315126100_JEXBIO_202_3_301C13","first-page":"185","article-title":"The 67 kDa spliced variant of beta-galactosidase serves as a reusable protective chaperone for tropoelastin","volume":"192","author":"Hinek","year":"1995","journal-title":"Ciba Foundation Symp"},{"key":"2024110713315126100_JEXBIO_202_3_301C14","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displaying the hydropathic character of a protein","volume":"157","author":"Kyte","year":"1982","journal-title":"J. Mol. Biol"},{"key":"2024110713315126100_JEXBIO_202_3_301C15","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1021\/ar00021a002","article-title":"Spider silk: the unravelling of a mystery","volume":"25","author":"Lewis","year":"1992","journal-title":"Acc. Chem. Res"},{"key":"2024110713315126100_JEXBIO_202_3_301C16","doi-asserted-by":"publisher","first-page":"23","DOI":"10.3109\/03008209409005632","article-title":"The effects of heating on the mechanical properties of arterial elastin","volume":"31","author":"Lillie","year":"1994","journal-title":"Connect. Tissue Res"},{"key":"2024110713315126100_JEXBIO_202_3_301C17","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1002\/(SICI)1097-0282(199611)39:5&lt;627::AID-BIP2&gt;3.0.CO;2-Y","article-title":"Elastin dehydration through the liquid and vapour phase: a comparison of osmotic stress models","volume":"39","author":"Lillie","year":"1996","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C18","doi-asserted-by":"publisher","first-page":"131","DOI":"10.3109\/03008209809028905","article-title":"Mechanical role of elastin-associated microfibrils in pig aortic elastic tissue","volume":"37","author":"Lillie","year":"1998","journal-title":"Connect. Tissue Res"},{"key":"2024110713315126100_JEXBIO_202_3_301C19","doi-asserted-by":"publisher","first-page":"1147","DOI":"10.1002\/bip.360290805","article-title":"The effects of hydration on the dynamic mechanical properties of elastin","volume":"29","author":"Lillie","year":"1990","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C20","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1002\/(SICI)1097-0282(199611)39:5&lt;641::AID-BIP3&gt;3.0.CO;2-W","article-title":"Swelling and viscoelastic properties of osmotically stressed elastin","volume":"39","author":"Lillie","year":"1996","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C21","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1021\/j100671a023","article-title":"Thermodynamics of elasticity in open systems. Elastin","volume":"75","author":"Mistrali","year":"1971","journal-title":"J. Phys. Chem"},{"key":"2024110713315126100_JEXBIO_202_3_301C22","first-page":"1773","article-title":"The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins","volume":"66","author":"Nemethy","year":"1962","journal-title":"J. Protein Chem"},{"key":"2024110713315126100_JEXBIO_202_3_301C23","doi-asserted-by":"publisher","first-page":"400","DOI":"10.1016\/0076-6879(86)27032-9","article-title":"Osmotic stress for the direct measurement of intermolecular forces","volume":"127","author":"Parsegian","year":"1986","journal-title":"Meth. Enzymol"},{"key":"2024110713315126100_JEXBIO_202_3_301C24","doi-asserted-by":"publisher","first-page":"1440","DOI":"10.1016\/S0021-9258(18)54095-3","article-title":"Characterization of lamprin, an unusual matrix protein from lamprey cartilage. Implications for evolution, structure, and assembly of elastin and other fibrillar proteins","volume":"268","author":"Robson","year":"1993","journal-title":"J. Biol. Chem"},{"key":"2024110713315126100_JEXBIO_202_3_301C25","doi-asserted-by":"publisher","first-page":"146s","DOI":"10.1111\/1523-1747.ep12546048","article-title":"Structure\u2013function relationships in the evolution of elastin","volume":"79","author":"Sage","year":"1982","journal-title":"J. Invest. Dermatol"},{"key":"2024110713315126100_JEXBIO_202_3_301C26","first-page":"291","article-title":"Evolution of elastin structure","volume-title":"In Elastin and Elastic Tissue","author":"Sage","year":"1976"},{"key":"2024110713315126100_JEXBIO_202_3_301C27","first-page":"313","article-title":"Studies on the evolution of elastin. Phylogenetic distribution","volume":"64B","author":"Sage","year":"1979","journal-title":"Comp. Biochem. Physiol"},{"key":"2024110713315126100_JEXBIO_202_3_301C28","first-page":"13","article-title":"Studies on the evolution of elastin. Histology","volume":"66B","author":"Sage","year":"1980","journal-title":"Comp. Biochem. Physiol"},{"key":"2024110713315126100_JEXBIO_202_3_301C29","first-page":"473","article-title":"Studies on the evolution of elastin. III. The ancestral protein","volume":"68B","author":"Sage","year":"1981","journal-title":"Comp. Biochem. Physiol"},{"key":"2024110713315126100_JEXBIO_202_3_301C30","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1021\/bk-1980-0127.ch013","article-title":"Density of elastin\u2013water systems","volume-title":"In Water in Polymers","author":"Scandola","year":"1980"},{"key":"2024110713315126100_JEXBIO_202_3_301C31","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1242\/jeb.114.1.239","article-title":"Physical and chemical properties of rubber-like elastic fibres from the octopus aorta","volume":"114","author":"Shadwick","year":"1985","journal-title":"J. Exp. Biol"},{"key":"2024110713315126100_JEXBIO_202_3_301C32","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1242\/jeb.114.1.259","article-title":"Mechanical properties of the octopus aorta","volume":"114","author":"Shadwick","year":"1985","journal-title":"J. Exp. Biol"},{"key":"2024110713315126100_JEXBIO_202_3_301C33","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1016\/0003-2697(76)90224-4","article-title":"Purification and composition of elastins from different animal species","volume":"74","author":"Starcher","year":"1976","journal-title":"Analyt. Biochem"},{"key":"2024110713315126100_JEXBIO_202_3_301C34","doi-asserted-by":"publisher","first-page":"85","DOI":"10.3109\/03008207409152092","article-title":"The isolation of chemically pure elastins in a form suitable for mechanical testing","volume":"2","author":"Steven","year":"1974","journal-title":"Connect. Tissue Res"},{"key":"2024110713315126100_JEXBIO_202_3_301C35","doi-asserted-by":"publisher","first-page":"4240","DOI":"10.1021\/ja00881a009","article-title":"Contributions of hydrophobic interactions to the stability of the globular conformations of proteins","volume":"84","author":"Tanford","year":"1962","journal-title":"J. Am. Chem. Soc"},{"key":"2024110713315126100_JEXBIO_202_3_301C36","volume-title":"The Hydrophobic Effect: Formation of Micelles and Biological Membranes","author":"Tanford","year":"1980"},{"key":"2024110713315126100_JEXBIO_202_3_301C37","doi-asserted-by":"publisher","first-page":"1243","DOI":"10.1002\/bip.360320913","article-title":"Hydrophobicity scale for proteins based on inverse temperature transitions","volume":"32","author":"Urry","year":"1992","journal-title":"Biopolymers"},{"key":"2024110713315126100_JEXBIO_202_3_301C38","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1111\/j.1399-3011.1969.tb01650.x","article-title":"Correlations between amino acid sequence and conformation of immunoglobin light chains. I. Hydrophobicity and fractional charge","volume":"1","author":"Welscher","year":"1969","journal-title":"Int. J. Protein Res"}],"container-title":["Journal of Experimental Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.biologists.com\/jeb\/article-pdf\/202\/3\/301\/3577923\/jexbio_202_3_301.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jeb\/article-pdf\/202\/3\/301\/3577923\/jexbio_202_3_301.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,11,7]],"date-time":"2024-11-07T13:32:08Z","timestamp":1730986328000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jeb\/article\/202\/3\/301\/8017\/The-hydrophobicity-of-vertebrate-elastins"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,2,1]]},"references-count":38,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1999,2,1]]}},"URL":"https:\/\/doi.org\/10.1242\/jeb.202.3.301","relation":{},"ISSN":["0022-0949","1477-9145"],"issn-type":[{"value":"0022-0949","type":"print"},{"value":"1477-9145","type":"electronic"}],"subject":[],"published":{"date-parts":[[1999,2,1]]}}}