Symmetry and Size of Membrane Protein Polyhedral Nanoparticles
In recent experiments [T. Basta et al., Proc. Natl. Acad. Sci. U.S.A. 111, 670 (2014)] lipids and membrane proteins were observed to self-assemble into membrane protein polyhedral nanoparticles (MPPNs) with a well-defined polyhedral protein arrangement and characteristic size. We develop a model of...
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Veröffentlicht in: | Physical review letters 2016-09, Vol.117 (13), p.138103-138103, Article 138103 |
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creator | Li, Di Kahraman, Osman Haselwandter, Christoph A |
description | In recent experiments [T. Basta et al., Proc. Natl. Acad. Sci. U.S.A. 111, 670 (2014)] lipids and membrane proteins were observed to self-assemble into membrane protein polyhedral nanoparticles (MPPNs) with a well-defined polyhedral protein arrangement and characteristic size. We develop a model of MPPN self-assembly in which the preferred symmetry and size of MPPNs emerge from the interplay of protein-induced lipid bilayer deformations, topological defects in protein packing, and thermal effects. With all model parameters determined directly from experiments, our model correctly predicts the observed symmetry and size of MPPNs. Our model suggests how key lipid and protein properties can be modified to produce a range of MPPN symmetries and sizes in experiments. |
doi_str_mv | 10.1103/PhysRevLett.117.138103 |
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Basta et al., Proc. Natl. Acad. Sci. U.S.A. 111, 670 (2014)] lipids and membrane proteins were observed to self-assemble into membrane protein polyhedral nanoparticles (MPPNs) with a well-defined polyhedral protein arrangement and characteristic size. We develop a model of MPPN self-assembly in which the preferred symmetry and size of MPPNs emerge from the interplay of protein-induced lipid bilayer deformations, topological defects in protein packing, and thermal effects. With all model parameters determined directly from experiments, our model correctly predicts the observed symmetry and size of MPPNs. 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Basta et al., Proc. Natl. Acad. Sci. U.S.A. 111, 670 (2014)] lipids and membrane proteins were observed to self-assemble into membrane protein polyhedral nanoparticles (MPPNs) with a well-defined polyhedral protein arrangement and characteristic size. We develop a model of MPPN self-assembly in which the preferred symmetry and size of MPPNs emerge from the interplay of protein-induced lipid bilayer deformations, topological defects in protein packing, and thermal effects. With all model parameters determined directly from experiments, our model correctly predicts the observed symmetry and size of MPPNs. Our model suggests how key lipid and protein properties can be modified to produce a range of MPPN symmetries and sizes in experiments.</description><subject>Deformation effects</subject><subject>Lipids</subject><subject>Mathematical models</subject><subject>Membranes</subject><subject>Nanoparticles</subject><subject>Proteins</subject><subject>Self assembly</subject><subject>Symmetry</subject><issn>0031-9007</issn><issn>1079-7114</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqNkN1LwzAUxYMobk7_hdFHXzpzk6ZJXgQZfsHU4fS5pMktq_RjJp1Q_3orm-KjTxcO55x7-BEyBToDoPxiue7DM34ssOsGQc6Aq0E-IGOgUscSIDkkY0o5xJpSOSInIbxRSoGl6piMmJQggKkxuVz1dY2d7yPTuGhVfmLUFtED1rk3DUZL33ZYNtGyrfo1Om-q6NE07cb4rrQVhlNyVJgq4Nn-TsjrzfXL_C5ePN3ez68WseWadXEhLEotLFBjXQ5UuDR3TmOuFSQ2YZZTKPSwtkgEE8rmXNFEK2eY4pbynE_I-a5349v3LYYuq8tgsaqGke02ZKASoUAwgH9YueCa6yQdrOnOan0bgsci2_iyNr7PgGbfmLM_mAdBZjvMQ3C6_7HNa3S_sR-u_AuIM3rl</recordid><startdate>20160923</startdate><enddate>20160923</enddate><creator>Li, Di</creator><creator>Kahraman, Osman</creator><creator>Haselwandter, Christoph A</creator><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7U5</scope><scope>8FD</scope><scope>H8D</scope><scope>L7M</scope></search><sort><creationdate>20160923</creationdate><title>Symmetry and Size of Membrane Protein Polyhedral Nanoparticles</title><author>Li, Di ; Kahraman, Osman ; Haselwandter, Christoph A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-f5ce795c10acdb105d6bdd9eb9814c42c301f9031f45258cb380498da283c03b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Deformation effects</topic><topic>Lipids</topic><topic>Mathematical models</topic><topic>Membranes</topic><topic>Nanoparticles</topic><topic>Proteins</topic><topic>Self assembly</topic><topic>Symmetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Di</creatorcontrib><creatorcontrib>Kahraman, Osman</creatorcontrib><creatorcontrib>Haselwandter, Christoph A</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Physical review letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Di</au><au>Kahraman, Osman</au><au>Haselwandter, Christoph A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Symmetry and Size of Membrane Protein Polyhedral Nanoparticles</atitle><jtitle>Physical review letters</jtitle><addtitle>Phys Rev Lett</addtitle><date>2016-09-23</date><risdate>2016</risdate><volume>117</volume><issue>13</issue><spage>138103</spage><epage>138103</epage><pages>138103-138103</pages><artnum>138103</artnum><issn>0031-9007</issn><eissn>1079-7114</eissn><abstract>In recent experiments [T. Basta et al., Proc. Natl. Acad. Sci. U.S.A. 111, 670 (2014)] lipids and membrane proteins were observed to self-assemble into membrane protein polyhedral nanoparticles (MPPNs) with a well-defined polyhedral protein arrangement and characteristic size. We develop a model of MPPN self-assembly in which the preferred symmetry and size of MPPNs emerge from the interplay of protein-induced lipid bilayer deformations, topological defects in protein packing, and thermal effects. With all model parameters determined directly from experiments, our model correctly predicts the observed symmetry and size of MPPNs. Our model suggests how key lipid and protein properties can be modified to produce a range of MPPN symmetries and sizes in experiments.</abstract><cop>United States</cop><pmid>27715128</pmid><doi>10.1103/PhysRevLett.117.138103</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Deformation effects Lipids Mathematical models Membranes Nanoparticles Proteins Self assembly Symmetry |
title | Symmetry and Size of Membrane Protein Polyhedral Nanoparticles |
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