Thermal-induced force release in oxyhemoglobin
Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the beh...
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| Veröffentlicht in: | Scientific reports 2015-08, Vol.5 (1), p.13064-13064, Article 13064 |
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| description | Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the behavior of the Young’s modulus and the internal friction for temperatures between 20 °C and 70 °C. We have found that around 49 °C oxyhemoglobin crystal samples undergo a sudden and strong increase of their Young’s modulus, accompanied by a sudden decrease of the internal friction. This sudden mechanical change (and the ensuing force release) takes place in a partially unfolded state and precedes the full denaturation transition at higher temperatures. After this transformation, the hemoglobin crystals have the same mechanical properties as their initial state at room temperatures. We conjecture that it can be relevant for explaining the oxygen-releasing function of native oxyhemoglobin when the temperature is increased, e.g. due to active sport. The effect is specific for the quaternary structure of hemoglobin and is absent for myoglobin with only one peptide sequence. |
| doi_str_mv | 10.1038/srep13064 |
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G. ; Allahverdyan, A. E. ; Gevorgyan, D. S. ; Hu, Chin-Kun</creator><creatorcontrib>Gevorkian, S. G. ; Allahverdyan, A. E. ; Gevorgyan, D. S. ; Hu, Chin-Kun</creatorcontrib><description>Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the behavior of the Young’s modulus and the internal friction for temperatures between 20 °C and 70 °C. We have found that around 49 °C oxyhemoglobin crystal samples undergo a sudden and strong increase of their Young’s modulus, accompanied by a sudden decrease of the internal friction. This sudden mechanical change (and the ensuing force release) takes place in a partially unfolded state and precedes the full denaturation transition at higher temperatures. After this transformation, the hemoglobin crystals have the same mechanical properties as their initial state at room temperatures. We conjecture that it can be relevant for explaining the oxygen-releasing function of native oxyhemoglobin when the temperature is increased, e.g. due to active sport. The effect is specific for the quaternary structure of hemoglobin and is absent for myoglobin with only one peptide sequence.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep13064</identifier><identifier>PMID: 26277901</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/337/470/2284 ; 631/57 ; 692/700/784 ; Algorithms ; Animals ; Crystallography, X-Ray ; Crystals ; Denaturation ; Elastic Modulus ; Hemoglobin ; Horses ; Humanities and Social Sciences ; Humans ; Mechanical properties ; multidisciplinary ; Myoglobins ; Oxygen ; Oxyhemoglobins - chemistry ; Oxyhemoglobins - metabolism ; Protein structure ; Protein Structure, Tertiary ; Quaternary structure ; Science ; Temperature ; Temperature effects</subject><ispartof>Scientific reports, 2015-08, Vol.5 (1), p.13064-13064, Article 13064</ispartof><rights>The Author(s) 2015</rights><rights>Copyright Nature Publishing Group Aug 2015</rights><rights>Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-aea03de34c1c9f4359dcd2809602e224f296e02341e1ecf04a830d5612d7e8833</citedby><cites>FETCH-LOGICAL-c438t-aea03de34c1c9f4359dcd2809602e224f296e02341e1ecf04a830d5612d7e8833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4538398/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4538398/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26277901$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gevorkian, S. G.</creatorcontrib><creatorcontrib>Allahverdyan, A. E.</creatorcontrib><creatorcontrib>Gevorgyan, D. S.</creatorcontrib><creatorcontrib>Hu, Chin-Kun</creatorcontrib><title>Thermal-induced force release in oxyhemoglobin</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the behavior of the Young’s modulus and the internal friction for temperatures between 20 °C and 70 °C. We have found that around 49 °C oxyhemoglobin crystal samples undergo a sudden and strong increase of their Young’s modulus, accompanied by a sudden decrease of the internal friction. This sudden mechanical change (and the ensuing force release) takes place in a partially unfolded state and precedes the full denaturation transition at higher temperatures. After this transformation, the hemoglobin crystals have the same mechanical properties as their initial state at room temperatures. We conjecture that it can be relevant for explaining the oxygen-releasing function of native oxyhemoglobin when the temperature is increased, e.g. due to active sport. 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G.</au><au>Allahverdyan, A. E.</au><au>Gevorgyan, D. S.</au><au>Hu, Chin-Kun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermal-induced force release in oxyhemoglobin</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2015-08-17</date><risdate>2015</risdate><volume>5</volume><issue>1</issue><spage>13064</spage><epage>13064</epage><pages>13064-13064</pages><artnum>13064</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Oxygen is released to living tissues via conformational changes of hemoglobin from R-state (oxyhemoglobin) to T-state (desoxyhemoglobin). The detailed mechanism of this process is not yet fully understood. We have carried out micromechanical experiments on oxyhemoglobin crystals to determine the behavior of the Young’s modulus and the internal friction for temperatures between 20 °C and 70 °C. We have found that around 49 °C oxyhemoglobin crystal samples undergo a sudden and strong increase of their Young’s modulus, accompanied by a sudden decrease of the internal friction. This sudden mechanical change (and the ensuing force release) takes place in a partially unfolded state and precedes the full denaturation transition at higher temperatures. After this transformation, the hemoglobin crystals have the same mechanical properties as their initial state at room temperatures. We conjecture that it can be relevant for explaining the oxygen-releasing function of native oxyhemoglobin when the temperature is increased, e.g. due to active sport. The effect is specific for the quaternary structure of hemoglobin and is absent for myoglobin with only one peptide sequence.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26277901</pmid><doi>10.1038/srep13064</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/337/470/2284 631/57 692/700/784 Algorithms Animals Crystallography, X-Ray Crystals Denaturation Elastic Modulus Hemoglobin Horses Humanities and Social Sciences Humans Mechanical properties multidisciplinary Myoglobins Oxygen Oxyhemoglobins - chemistry Oxyhemoglobins - metabolism Protein structure Protein Structure, Tertiary Quaternary structure Science Temperature Temperature effects |
| title | Thermal-induced force release in oxyhemoglobin |
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