Structural Order of Lipids and Proteins in Membranes: Evaluation of Fluorescence Anisotropy Data
The limiting long-time value of fluorescence anisotropy in membranes is correlated with the orientational order parameter, which characterizes the structural anisotropy of membranes. Existing experimental results for diphenylhexatriene in lipid bilayers are evaluated for the order parameter of lipid...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1979-12, Vol.76 (12), p.6361-6365 |
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| container_end_page | 6365 |
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| container_issue | 12 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 76 |
| creator | Jähnig, Fritz |
| description | The limiting long-time value of fluorescence anisotropy in membranes is correlated with the orientational order parameter, which characterizes the structural anisotropy of membranes. Existing experimental results for diphenylhexatriene in lipid bilayers are evaluated for the order parameter of lipid order. Steady-state measurements of fluorescence anisotropy can provide the order parameter in good approximation. Proteins in a fluid lipid phase increase the lipid order parameter so determined. Upon comparison with the order parameter from deuterium magnetic resonance, it is concluded that proteins increase the order of the surrounding lipids in off-normal directions. Order parameters of protein order obtained from the limiting value of protein fluorescence anisotropy are discussed with respect to the influence of lipid order on protein order. |
| doi_str_mv | 10.1073/pnas.76.12.6361 |
| format | Article |
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Existing experimental results for diphenylhexatriene in lipid bilayers are evaluated for the order parameter of lipid order. Steady-state measurements of fluorescence anisotropy can provide the order parameter in good approximation. Proteins in a fluid lipid phase increase the lipid order parameter so determined. Upon comparison with the order parameter from deuterium magnetic resonance, it is concluded that proteins increase the order of the surrounding lipids in off-normal directions. Order parameters of protein order obtained from the limiting value of protein fluorescence anisotropy are discussed with respect to the influence of lipid order on protein order.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.76.12.6361</identifier><identifier>PMID: 42914</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Anisotropy ; Biochemistry ; Cell membranes ; Chromophores ; Equilibrium flow ; Fluorescence ; Fluorescence Polarization ; Hydrogen-Ion Concentration ; Kinetics ; Lipids ; Membrane Fluidity ; Membrane Lipids - physiology ; Membrane Proteins - physiology ; Membranes - ultrastructure ; Models, Theoretical ; Molecules ; Motion ; Polarized light ; Rotation ; Temperature</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1979-12, Vol.76 (12), p.6361-6365</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-fb38b747b5821957a93c1c8d92e824b3ec9b3751dd96fe219c029d7e967ac98f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/76/12.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/70240$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/70240$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53770,53772,57996,58229</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/42914$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jähnig, Fritz</creatorcontrib><title>Structural Order of Lipids and Proteins in Membranes: Evaluation of Fluorescence Anisotropy Data</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The limiting long-time value of fluorescence anisotropy in membranes is correlated with the orientational order parameter, which characterizes the structural anisotropy of membranes. Existing experimental results for diphenylhexatriene in lipid bilayers are evaluated for the order parameter of lipid order. Steady-state measurements of fluorescence anisotropy can provide the order parameter in good approximation. Proteins in a fluid lipid phase increase the lipid order parameter so determined. Upon comparison with the order parameter from deuterium magnetic resonance, it is concluded that proteins increase the order of the surrounding lipids in off-normal directions. Order parameters of protein order obtained from the limiting value of protein fluorescence anisotropy are discussed with respect to the influence of lipid order on protein order.</description><subject>Anisotropy</subject><subject>Biochemistry</subject><subject>Cell membranes</subject><subject>Chromophores</subject><subject>Equilibrium flow</subject><subject>Fluorescence</subject><subject>Fluorescence Polarization</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Lipids</subject><subject>Membrane Fluidity</subject><subject>Membrane Lipids - physiology</subject><subject>Membrane Proteins - physiology</subject><subject>Membranes - ultrastructure</subject><subject>Models, Theoretical</subject><subject>Molecules</subject><subject>Motion</subject><subject>Polarized light</subject><subject>Rotation</subject><subject>Temperature</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtv1DAUhS1EBUPLGgkk5BWsMrUdx49KLKo-kaZqpcLaOI4DrjJ2sJ2q_fc4naEtG1Z3cb5z7z06ALzDaIkRr_dHr9OSsyUmS1Yz_AIsMJK4YlSil2CBEOGVoIS-Bm9SukEIyUagV2CHEonpAvy4znEyeYp6gJexsxGGHq7c6LoEte_gVQzZOp-g8_DCrtuovU0H8ORWD5POLviZPx2mEG0y1hsLD71LIccw3sNjnfUe2On1kOzb7dwF309Pvh2dV6vLs69Hh6vKNKTJVd_WouWUt40gWDZcy9pgIzpJrCC0ra2Rbc0b3HWS9bYgBhHZcSsZ10aKvt4FXzZ7x6ld2678kksmNUa31vFeBe3Uv4p3v9TPcKsoxoLR4v-09cfwe7Ipq7UriYahBA5TUpwKTlkzg_sb0MSQUrT94w2M1NyImhtRnClM1NxIcXx4_toj_1BBUT9v1dn2V3uyq34ahmzvciE__pcswPsNcJNyiE8EIhTVfwBRt6or</recordid><startdate>19791201</startdate><enddate>19791201</enddate><creator>Jähnig, Fritz</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>19791201</creationdate><title>Structural Order of Lipids and Proteins in Membranes: Evaluation of Fluorescence Anisotropy Data</title><author>Jähnig, Fritz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-fb38b747b5821957a93c1c8d92e824b3ec9b3751dd96fe219c029d7e967ac98f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Anisotropy</topic><topic>Biochemistry</topic><topic>Cell membranes</topic><topic>Chromophores</topic><topic>Equilibrium flow</topic><topic>Fluorescence</topic><topic>Fluorescence Polarization</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Lipids</topic><topic>Membrane Fluidity</topic><topic>Membrane Lipids - physiology</topic><topic>Membrane Proteins - physiology</topic><topic>Membranes - ultrastructure</topic><topic>Models, Theoretical</topic><topic>Molecules</topic><topic>Motion</topic><topic>Polarized light</topic><topic>Rotation</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jähnig, Fritz</creatorcontrib><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>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jähnig, Fritz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Order of Lipids and Proteins in Membranes: Evaluation of Fluorescence Anisotropy Data</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1979-12-01</date><risdate>1979</risdate><volume>76</volume><issue>12</issue><spage>6361</spage><epage>6365</epage><pages>6361-6365</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The limiting long-time value of fluorescence anisotropy in membranes is correlated with the orientational order parameter, which characterizes the structural anisotropy of membranes. Existing experimental results for diphenylhexatriene in lipid bilayers are evaluated for the order parameter of lipid order. Steady-state measurements of fluorescence anisotropy can provide the order parameter in good approximation. Proteins in a fluid lipid phase increase the lipid order parameter so determined. Upon comparison with the order parameter from deuterium magnetic resonance, it is concluded that proteins increase the order of the surrounding lipids in off-normal directions. Order parameters of protein order obtained from the limiting value of protein fluorescence anisotropy are discussed with respect to the influence of lipid order on protein order.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>42914</pmid><doi>10.1073/pnas.76.12.6361</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1979-12, Vol.76 (12), p.6361-6365 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Anisotropy Biochemistry Cell membranes Chromophores Equilibrium flow Fluorescence Fluorescence Polarization Hydrogen-Ion Concentration Kinetics Lipids Membrane Fluidity Membrane Lipids - physiology Membrane Proteins - physiology Membranes - ultrastructure Models, Theoretical Molecules Motion Polarized light Rotation Temperature |
| title | Structural Order of Lipids and Proteins in Membranes: Evaluation of Fluorescence Anisotropy Data |
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