Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers
Reconstituted lipid bilayers of dimyristoylphosphatidylcholine (DMPC) and gramicidin A' have been prepared by cosolubilizing gramicidin and DMPC in one of three organic solvent systems followed by vacuum drying and hydration. The conformational state of gramicidin as characterized by 23Na NMR,...
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| Veröffentlicht in: | Biophysical journal 1988-08, Vol.54 (2), p.259-267 |
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| creator | LoGrasso, P.V. Moll, F. Cross, T.A. |
| description | Reconstituted lipid bilayers of dimyristoylphosphatidylcholine (DMPC) and gramicidin A' have been prepared by cosolubilizing gramicidin and DMPC in one of three organic solvent systems followed by vacuum drying and hydration. The conformational state of gramicidin as characterized by 23Na NMR, circular dichroism, and solid state 15N NMR is dependent upon the cosolubilizing solvent system. In particular, two conformational states are described; a state in which Na+ has minimal interactions with the polypeptide, referred to as a nonchannel state, and a state in which Na+ interacts very strongly with the polypeptide, referred to as the channel state. Both of these conformations are intimately associated with the hydrophobic core of the lipid bilayer. Furthermore, both of these states are stable in the bilayer at neutral pH and at a temperature above the bilayer phase transition temperature. These results with gramicidin suggest that the conformation of membrane proteins may be dictated by the conformation before membrane insertion and may be dependent upon the mechanism by which the insertion is accomplished. |
| doi_str_mv | 10.1016/S0006-3495(88)82955-2 |
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The conformational state of gramicidin as characterized by 23Na NMR, circular dichroism, and solid state 15N NMR is dependent upon the cosolubilizing solvent system. In particular, two conformational states are described; a state in which Na+ has minimal interactions with the polypeptide, referred to as a nonchannel state, and a state in which Na+ interacts very strongly with the polypeptide, referred to as the channel state. Both of these conformations are intimately associated with the hydrophobic core of the lipid bilayer. Furthermore, both of these states are stable in the bilayer at neutral pH and at a temperature above the bilayer phase transition temperature. These results with gramicidin suggest that the conformation of membrane proteins may be dictated by the conformation before membrane insertion and may be dependent upon the mechanism by which the insertion is accomplished.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(88)82955-2</identifier><identifier>PMID: 2462923</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Biological and medical sciences ; Circular Dichroism ; Dimyristoylphosphatidylcholine ; Fundamental and applied biological sciences. Psychology ; Gramicidin ; Lipid Bilayers ; Magnetic Resonance Spectroscopy ; Models, Biological ; Molecular biophysics ; Molecular Conformation ; Solvents ; Structure in molecular biology ; Tridimensional structure</subject><ispartof>Biophysical journal, 1988-08, Vol.54 (2), p.259-267</ispartof><rights>1988 The Biophysical Society</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-f0d265f906352dd7676766b8802855f52a74592040f16146c94f8f43c97956db3</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/PMC1330292/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(88)82955-2$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7263497$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2462923$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LoGrasso, P.V.</creatorcontrib><creatorcontrib>Moll, F.</creatorcontrib><creatorcontrib>Cross, T.A.</creatorcontrib><title>Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Reconstituted lipid bilayers of dimyristoylphosphatidylcholine (DMPC) and gramicidin A' have been prepared by cosolubilizing gramicidin and DMPC in one of three organic solvent systems followed by vacuum drying and hydration. The conformational state of gramicidin as characterized by 23Na NMR, circular dichroism, and solid state 15N NMR is dependent upon the cosolubilizing solvent system. In particular, two conformational states are described; a state in which Na+ has minimal interactions with the polypeptide, referred to as a nonchannel state, and a state in which Na+ interacts very strongly with the polypeptide, referred to as the channel state. Both of these conformations are intimately associated with the hydrophobic core of the lipid bilayer. Furthermore, both of these states are stable in the bilayer at neutral pH and at a temperature above the bilayer phase transition temperature. These results with gramicidin suggest that the conformation of membrane proteins may be dictated by the conformation before membrane insertion and may be dependent upon the mechanism by which the insertion is accomplished.</description><subject>Biological and medical sciences</subject><subject>Circular Dichroism</subject><subject>Dimyristoylphosphatidylcholine</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gramicidin</subject><subject>Lipid Bilayers</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Biological</subject><subject>Molecular biophysics</subject><subject>Molecular Conformation</subject><subject>Solvents</subject><subject>Structure in molecular biology</subject><subject>Tridimensional structure</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvEzEUhS0EKiHwEyp5gRAshl57xh7PhqqqgFaq1EVgbTl-NBfN2MGeRMq_Z6aJIlghLyz5fL6Pcwi5ZPCZAZNXKwCQVd104qNSnxTvhKj4C7JgouEVgJIvyeKMvCZvSvkFwLgAdkEueCN5x-sFWa1Sv_dxpBssY8oH6vzWR-ej9TQF-pTNgBYdRnpDbYoh5cGMmGKh09Pm4LIZvaM9btHRNfbm4HN5S14F0xf_7nQvyc9vX3_c3lUPj9_vb28eKitEO1YBHJcidCBrwZ1r5XzkWingSogguGkb0XFoIDDJGmm7JqjQ1LZrOyHdul6SL8e629168M5Oa2TT623GweSDTgb1v0rEjX5Ke83qGub1l-TDqUBOv3e-jHrAYn3fm-jTruhWSeCthAkUR9DmVEr24dyEgZ7T0M9p6NlqrZR-TkPPDS7_nvD862T_pL8_6aZY04dsosVyxloup4rthF0fMT-5uUefdbE4R-Qweztql_A_g_wBdxCm9w</recordid><startdate>19880801</startdate><enddate>19880801</enddate><creator>LoGrasso, P.V.</creator><creator>Moll, F.</creator><creator>Cross, T.A.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>19880801</creationdate><title>Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers</title><author>LoGrasso, P.V. ; Moll, F. ; Cross, T.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-f0d265f906352dd7676766b8802855f52a74592040f16146c94f8f43c97956db3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Biological and medical sciences</topic><topic>Circular Dichroism</topic><topic>Dimyristoylphosphatidylcholine</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gramicidin</topic><topic>Lipid Bilayers</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Biological</topic><topic>Molecular biophysics</topic><topic>Molecular Conformation</topic><topic>Solvents</topic><topic>Structure in molecular biology</topic><topic>Tridimensional structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LoGrasso, P.V.</creatorcontrib><creatorcontrib>Moll, F.</creatorcontrib><creatorcontrib>Cross, T.A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</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>LoGrasso, P.V.</au><au>Moll, F.</au><au>Cross, T.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1988-08-01</date><risdate>1988</risdate><volume>54</volume><issue>2</issue><spage>259</spage><epage>267</epage><pages>259-267</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>Reconstituted lipid bilayers of dimyristoylphosphatidylcholine (DMPC) and gramicidin A' have been prepared by cosolubilizing gramicidin and DMPC in one of three organic solvent systems followed by vacuum drying and hydration. The conformational state of gramicidin as characterized by 23Na NMR, circular dichroism, and solid state 15N NMR is dependent upon the cosolubilizing solvent system. In particular, two conformational states are described; a state in which Na+ has minimal interactions with the polypeptide, referred to as a nonchannel state, and a state in which Na+ interacts very strongly with the polypeptide, referred to as the channel state. Both of these conformations are intimately associated with the hydrophobic core of the lipid bilayer. Furthermore, both of these states are stable in the bilayer at neutral pH and at a temperature above the bilayer phase transition temperature. These results with gramicidin suggest that the conformation of membrane proteins may be dictated by the conformation before membrane insertion and may be dependent upon the mechanism by which the insertion is accomplished.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2462923</pmid><doi>10.1016/S0006-3495(88)82955-2</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 1988-08, Vol.54 (2), p.259-267 |
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| language | eng |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Biological and medical sciences Circular Dichroism Dimyristoylphosphatidylcholine Fundamental and applied biological sciences. Psychology Gramicidin Lipid Bilayers Magnetic Resonance Spectroscopy Models, Biological Molecular biophysics Molecular Conformation Solvents Structure in molecular biology Tridimensional structure |
| title | Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers |
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