Relaxation Behavior of Collagen
The dynamic mechanical properties of purified collagen from bovine tendon were studied using a torsion pendulum in the temperature range of 120°-360°K at 0.3–1 cps. In the temperature range studied, two loss peaks were observed: a β-peak at about 200°K, and an α-peak approximately five times larger...
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| Veröffentlicht in: | Biophysical journal 1973-08, Vol.13 (8), p.772-779 |
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| container_title | Biophysical journal |
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| creator | Stefanou, H. Woodward, A.E. Morrow, Darrell |
| description | The dynamic mechanical properties of purified collagen from bovine tendon were studied using a torsion pendulum in the temperature range of 120°-360°K at 0.3–1 cps. In the temperature range studied, two loss peaks were observed: a β-peak at about 200°K, and an α-peak approximately five times larger at about 280°K. The temperature of the α-transition is shown to be dependent on water content, decreasing with increasing amount of water and shifting to lower temperatures. Broad-line proton magnetic resonance results were also obtained on similar samples. A narrow nuclear magnetic resonance (NMR) line appears at about 250°C. The effects of shrinkage to form gelatin and of cross-linking on the relaxation behavior of collagen were also studied. The motions taking place in collagen over the 120°-360°K range are discussed. |
| doi_str_mv | 10.1016/S0006-3495(73)86023-0 |
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In the temperature range studied, two loss peaks were observed: a β-peak at about 200°K, and an α-peak approximately five times larger at about 280°K. The temperature of the α-transition is shown to be dependent on water content, decreasing with increasing amount of water and shifting to lower temperatures. Broad-line proton magnetic resonance results were also obtained on similar samples. A narrow nuclear magnetic resonance (NMR) line appears at about 250°C. The effects of shrinkage to form gelatin and of cross-linking on the relaxation behavior of collagen were also studied. The motions taking place in collagen over the 120°-360°K range are discussed.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(73)86023-0</identifier><identifier>PMID: 4737857</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cattle ; Collagen ; Elasticity ; Formaldehyde ; Gelatin - analysis ; Hot Temperature ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Protein Denaturation ; Temperature ; Tendons ; Water ; X-Ray Diffraction</subject><ispartof>Biophysical journal, 1973-08, Vol.13 (8), p.772-779</ispartof><rights>1973 The Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-3dad557e254a75ad54c7ccdd87e9926f808684a70902bf1125ba1793a34bc7b23</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1484335/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349573860230$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3537,27901,27902,53766,53768,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4737857$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stefanou, H.</creatorcontrib><creatorcontrib>Woodward, A.E.</creatorcontrib><creatorcontrib>Morrow, Darrell</creatorcontrib><title>Relaxation Behavior of Collagen</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The dynamic mechanical properties of purified collagen from bovine tendon were studied using a torsion pendulum in the temperature range of 120°-360°K at 0.3–1 cps. In the temperature range studied, two loss peaks were observed: a β-peak at about 200°K, and an α-peak approximately five times larger at about 280°K. The temperature of the α-transition is shown to be dependent on water content, decreasing with increasing amount of water and shifting to lower temperatures. Broad-line proton magnetic resonance results were also obtained on similar samples. A narrow nuclear magnetic resonance (NMR) line appears at about 250°C. The effects of shrinkage to form gelatin and of cross-linking on the relaxation behavior of collagen were also studied. The motions taking place in collagen over the 120°-360°K range are discussed.</description><subject>Animals</subject><subject>Cattle</subject><subject>Collagen</subject><subject>Elasticity</subject><subject>Formaldehyde</subject><subject>Gelatin - analysis</subject><subject>Hot Temperature</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Temperature</subject><subject>Tendons</subject><subject>Water</subject><subject>X-Ray Diffraction</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEUhYMotVZ_QrEr0cVoMnnORtHiCwTBxzpkMnfayHSiybTovze1pejKVQLn3HPP_RAaEnxKMBFnzxhjkVFW8GNJT5TAOc3wFuoTzvIMYyW2UX9j2UV7Mb5hTHKOSQ_1mKRScdlHh0_QmE_TOd-OrmBqFs6Hka9HY980ZgLtPtqpTRPhYP0O0OvN9cv4Lnt4vL0fXz5klom8y2hlKs4l5JwZydOfWWltVSkJRZGLWqU-Kkm4wHlZk1SjNEQW1FBWWlnmdIDOV7nv83IGlYW2C6bR78HNTPjS3jj9V2ndVE_8QhOmGKU8BRytA4L_mEPs9MxFC-mKFvw8akWKQnAlkpGvjDb4GAPUmyUE6yVZ_UNWL7FpSfUPWY3T3PB3w83UGmXSL1Y6JEwLB0FH66C1ULkAttOVd_9s-AZpjYeb</recordid><startdate>19730801</startdate><enddate>19730801</enddate><creator>Stefanou, H.</creator><creator>Woodward, A.E.</creator><creator>Morrow, Darrell</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19730801</creationdate><title>Relaxation Behavior of Collagen</title><author>Stefanou, H. ; Woodward, A.E. ; Morrow, Darrell</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-3dad557e254a75ad54c7ccdd87e9926f808684a70902bf1125ba1793a34bc7b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Animals</topic><topic>Cattle</topic><topic>Collagen</topic><topic>Elasticity</topic><topic>Formaldehyde</topic><topic>Gelatin - analysis</topic><topic>Hot Temperature</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Temperature</topic><topic>Tendons</topic><topic>Water</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stefanou, H.</creatorcontrib><creatorcontrib>Woodward, A.E.</creatorcontrib><creatorcontrib>Morrow, Darrell</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stefanou, H.</au><au>Woodward, A.E.</au><au>Morrow, Darrell</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Relaxation Behavior of Collagen</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1973-08-01</date><risdate>1973</risdate><volume>13</volume><issue>8</issue><spage>772</spage><epage>779</epage><pages>772-779</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The dynamic mechanical properties of purified collagen from bovine tendon were studied using a torsion pendulum in the temperature range of 120°-360°K at 0.3–1 cps. In the temperature range studied, two loss peaks were observed: a β-peak at about 200°K, and an α-peak approximately five times larger at about 280°K. The temperature of the α-transition is shown to be dependent on water content, decreasing with increasing amount of water and shifting to lower temperatures. Broad-line proton magnetic resonance results were also obtained on similar samples. A narrow nuclear magnetic resonance (NMR) line appears at about 250°C. The effects of shrinkage to form gelatin and of cross-linking on the relaxation behavior of collagen were also studied. The motions taking place in collagen over the 120°-360°K range are discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4737857</pmid><doi>10.1016/S0006-3495(73)86023-0</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Animals Cattle Collagen Elasticity Formaldehyde Gelatin - analysis Hot Temperature Magnetic Resonance Spectroscopy Protein Conformation Protein Denaturation Temperature Tendons Water X-Ray Diffraction |
| title | Relaxation Behavior of Collagen |
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