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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Physical review letters 2016-09, Vol.117 (13), p.138103-138103, Article 138103
Hauptverfasser: Li, Di, Kahraman, Osman, Haselwandter, Christoph A
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 138103
container_issue 13
container_start_page 138103
container_title Physical review letters
container_volume 117
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
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1845815211</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1835393946</sourcerecordid><originalsourceid>FETCH-LOGICAL-c392t-f5ce795c10acdb105d6bdd9eb9814c42c301f9031f45258cb380498da283c03b3</originalsourceid><addsrcrecordid>eNqNkN1LwzAUxYMobk7_hdFHXzpzk6ZJXgQZfsHU4fS5pMktq_RjJp1Q_3orm-KjTxcO55x7-BEyBToDoPxiue7DM34ssOsGQc6Aq0E-IGOgUscSIDkkY0o5xJpSOSInIbxRSoGl6piMmJQggKkxuVz1dY2d7yPTuGhVfmLUFtED1rk3DUZL33ZYNtGyrfo1Om-q6NE07cb4rrQVhlNyVJgq4Nn-TsjrzfXL_C5ePN3ez68WseWadXEhLEotLFBjXQ5UuDR3TmOuFSQ2YZZTKPSwtkgEE8rmXNFEK2eY4pbynE_I-a5349v3LYYuq8tgsaqGke02ZKASoUAwgH9YueCa6yQdrOnOan0bgsci2_iyNr7PgGbfmLM_mAdBZjvMQ3C6_7HNa3S_sR-u_AuIM3rl</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1835393946</pqid></control><display><type>article</type><title>Symmetry and Size of Membrane Protein Polyhedral Nanoparticles</title><source>American Physical Society Journals</source><creator>Li, Di ; Kahraman, Osman ; Haselwandter, Christoph A</creator><creatorcontrib>Li, Di ; Kahraman, Osman ; Haselwandter, Christoph A</creatorcontrib><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.</description><identifier>ISSN: 0031-9007</identifier><identifier>EISSN: 1079-7114</identifier><identifier>DOI: 10.1103/PhysRevLett.117.138103</identifier><identifier>PMID: 27715128</identifier><language>eng</language><publisher>United States</publisher><subject>Deformation effects ; Lipids ; Mathematical models ; Membranes ; Nanoparticles ; Proteins ; Self assembly ; Symmetry</subject><ispartof>Physical review letters, 2016-09, Vol.117 (13), p.138103-138103, Article 138103</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-f5ce795c10acdb105d6bdd9eb9814c42c301f9031f45258cb380498da283c03b3</citedby><cites>FETCH-LOGICAL-c392t-f5ce795c10acdb105d6bdd9eb9814c42c301f9031f45258cb380498da283c03b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,2863,2864,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27715128$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Di</creatorcontrib><creatorcontrib>Kahraman, Osman</creatorcontrib><creatorcontrib>Haselwandter, Christoph A</creatorcontrib><title>Symmetry and Size of Membrane Protein Polyhedral Nanoparticles</title><title>Physical review letters</title><addtitle>Phys Rev Lett</addtitle><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.</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>
fulltext fulltext
identifier ISSN: 0031-9007
ispartof Physical review letters, 2016-09, Vol.117 (13), p.138103-138103, Article 138103
issn 0031-9007
1079-7114
language eng
recordid cdi_proquest_miscellaneous_1845815211
source American Physical Society Journals
subjects Deformation effects
Lipids
Mathematical models
Membranes
Nanoparticles
Proteins
Self assembly
Symmetry
title Symmetry and Size of Membrane Protein Polyhedral Nanoparticles
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T06%3A53%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Symmetry%20and%20Size%20of%20Membrane%20Protein%20Polyhedral%20Nanoparticles&rft.jtitle=Physical%20review%20letters&rft.au=Li,%20Di&rft.date=2016-09-23&rft.volume=117&rft.issue=13&rft.spage=138103&rft.epage=138103&rft.pages=138103-138103&rft.artnum=138103&rft.issn=0031-9007&rft.eissn=1079-7114&rft_id=info:doi/10.1103/PhysRevLett.117.138103&rft_dat=%3Cproquest_cross%3E1835393946%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1835393946&rft_id=info:pmid/27715128&rfr_iscdi=true