Using symmetry to drive new protein assemblies

Recent improvements in de novo protein design are likely to support a broad range of applications, but larger complexes will be easier to create if a building block approach is adopted. Now protein filaments with tunable geometry can be made using assemblies that have both cyclic and superhelical sy...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nature chemistry 2023-12, Vol.15 (12), p.1653-1654
1. Verfasser: Tame, Jeremy R. H.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 1654
container_issue 12
container_start_page 1653
container_title Nature chemistry
container_volume 15
creator Tame, Jeremy R. H.
description Recent improvements in de novo protein design are likely to support a broad range of applications, but larger complexes will be easier to create if a building block approach is adopted. Now protein filaments with tunable geometry can be made using assemblies that have both cyclic and superhelical symmetries aligned along the same axis.
doi_str_mv 10.1038/s41557-023-01369-w
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2896809103</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2896809103</sourcerecordid><originalsourceid>FETCH-LOGICAL-c303t-17e9c7741b83e94beb7ffac8c49ebbb54afeaaabd48ebf21b6becf0a2f4304d73</originalsourceid><addsrcrecordid>eNp9kE1LAzEQhoMoWKt_wNOCFy9bk02y2Ryl-AUFL_YcknRStuxHzWwt_femrih48DRzeN6XmYeQa0ZnjPLqDgWTUuW04DllvNT5_oRMmJIyF1zo05-d03NygbihtJSclRMyW2LdrTM8tC0M8ZANfbaK9QdkHeyzbewHqLvMIkLrmhrwkpwF2yBcfc8pWT4-vM2f88Xr08v8fpF7TvmQMwXaKyWYqzho4cCpEKyvvNDgnJPCBrDWupWowIWCudKBD9QWQXAqVopPye3Ym0543wEOpq3RQ9PYDvodmqLSZUV1-j2hN3_QTb-LXbruSCkpCqpYooqR8rFHjBDMNtatjQfDqDkqNKNCkxSaL4Vmn0J8DGGCuzXE3-p_Up8sfXU8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2897542071</pqid></control><display><type>article</type><title>Using symmetry to drive new protein assemblies</title><source>SpringerLink Journals</source><source>Nature Journals Online</source><creator>Tame, Jeremy R. H.</creator><creatorcontrib>Tame, Jeremy R. H.</creatorcontrib><description>Recent improvements in de novo protein design are likely to support a broad range of applications, but larger complexes will be easier to create if a building block approach is adopted. Now protein filaments with tunable geometry can be made using assemblies that have both cyclic and superhelical symmetries aligned along the same axis.</description><identifier>ISSN: 1755-4330</identifier><identifier>EISSN: 1755-4349</identifier><identifier>DOI: 10.1038/s41557-023-01369-w</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/114/469 ; 631/57/2266 ; Analytical Chemistry ; Assemblies ; Biochemistry ; Chemistry ; Chemistry and Materials Science ; Chemistry/Food Science ; Design ; Filaments ; Inorganic Chemistry ; News &amp; Views ; news-and-views ; Organic Chemistry ; Physical Chemistry ; Polypeptides ; Proteins ; Superhelical DNA ; Symmetry</subject><ispartof>Nature chemistry, 2023-12, Vol.15 (12), p.1653-1654</ispartof><rights>Springer Nature Limited 2023</rights><rights>Springer Nature Limited 2023.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c303t-17e9c7741b83e94beb7ffac8c49ebbb54afeaaabd48ebf21b6becf0a2f4304d73</cites><orcidid>0000-0002-9341-7280</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41557-023-01369-w$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41557-023-01369-w$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Tame, Jeremy R. H.</creatorcontrib><title>Using symmetry to drive new protein assemblies</title><title>Nature chemistry</title><addtitle>Nat. Chem</addtitle><description>Recent improvements in de novo protein design are likely to support a broad range of applications, but larger complexes will be easier to create if a building block approach is adopted. Now protein filaments with tunable geometry can be made using assemblies that have both cyclic and superhelical symmetries aligned along the same axis.</description><subject>631/114/469</subject><subject>631/57/2266</subject><subject>Analytical Chemistry</subject><subject>Assemblies</subject><subject>Biochemistry</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemistry/Food Science</subject><subject>Design</subject><subject>Filaments</subject><subject>Inorganic Chemistry</subject><subject>News &amp; Views</subject><subject>news-and-views</subject><subject>Organic Chemistry</subject><subject>Physical Chemistry</subject><subject>Polypeptides</subject><subject>Proteins</subject><subject>Superhelical DNA</subject><subject>Symmetry</subject><issn>1755-4330</issn><issn>1755-4349</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp9kE1LAzEQhoMoWKt_wNOCFy9bk02y2Ryl-AUFL_YcknRStuxHzWwt_femrih48DRzeN6XmYeQa0ZnjPLqDgWTUuW04DllvNT5_oRMmJIyF1zo05-d03NygbihtJSclRMyW2LdrTM8tC0M8ZANfbaK9QdkHeyzbewHqLvMIkLrmhrwkpwF2yBcfc8pWT4-vM2f88Xr08v8fpF7TvmQMwXaKyWYqzho4cCpEKyvvNDgnJPCBrDWupWowIWCudKBD9QWQXAqVopPye3Ym0543wEOpq3RQ9PYDvodmqLSZUV1-j2hN3_QTb-LXbruSCkpCqpYooqR8rFHjBDMNtatjQfDqDkqNKNCkxSaL4Vmn0J8DGGCuzXE3-p_Up8sfXU8</recordid><startdate>20231201</startdate><enddate>20231201</enddate><creator>Tame, Jeremy R. H.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QR</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PDBOC</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-9341-7280</orcidid></search><sort><creationdate>20231201</creationdate><title>Using symmetry to drive new protein assemblies</title><author>Tame, Jeremy R. H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c303t-17e9c7741b83e94beb7ffac8c49ebbb54afeaaabd48ebf21b6becf0a2f4304d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>631/114/469</topic><topic>631/57/2266</topic><topic>Analytical Chemistry</topic><topic>Assemblies</topic><topic>Biochemistry</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemistry/Food Science</topic><topic>Design</topic><topic>Filaments</topic><topic>Inorganic Chemistry</topic><topic>News &amp; Views</topic><topic>news-and-views</topic><topic>Organic Chemistry</topic><topic>Physical Chemistry</topic><topic>Polypeptides</topic><topic>Proteins</topic><topic>Superhelical DNA</topic><topic>Symmetry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tame, Jeremy R. H.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Chemoreception Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection (ProQuest)</collection><collection>Natural Science Collection (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Materials Science Collection</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health &amp; Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health &amp; Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied &amp; Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><jtitle>Nature chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tame, Jeremy R. H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Using symmetry to drive new protein assemblies</atitle><jtitle>Nature chemistry</jtitle><stitle>Nat. Chem</stitle><date>2023-12-01</date><risdate>2023</risdate><volume>15</volume><issue>12</issue><spage>1653</spage><epage>1654</epage><pages>1653-1654</pages><issn>1755-4330</issn><eissn>1755-4349</eissn><abstract>Recent improvements in de novo protein design are likely to support a broad range of applications, but larger complexes will be easier to create if a building block approach is adopted. Now protein filaments with tunable geometry can be made using assemblies that have both cyclic and superhelical symmetries aligned along the same axis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><doi>10.1038/s41557-023-01369-w</doi><tpages>2</tpages><orcidid>https://orcid.org/0000-0002-9341-7280</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 1755-4330
ispartof Nature chemistry, 2023-12, Vol.15 (12), p.1653-1654
issn 1755-4330
1755-4349
language eng
recordid cdi_proquest_miscellaneous_2896809103
source SpringerLink Journals; Nature Journals Online
subjects 631/114/469
631/57/2266
Analytical Chemistry
Assemblies
Biochemistry
Chemistry
Chemistry and Materials Science
Chemistry/Food Science
Design
Filaments
Inorganic Chemistry
News & Views
news-and-views
Organic Chemistry
Physical Chemistry
Polypeptides
Proteins
Superhelical DNA
Symmetry
title Using symmetry to drive new protein assemblies
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T00%3A41%3A00IST&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=Using%20symmetry%20to%20drive%20new%20protein%20assemblies&rft.jtitle=Nature%20chemistry&rft.au=Tame,%20Jeremy%20R.%20H.&rft.date=2023-12-01&rft.volume=15&rft.issue=12&rft.spage=1653&rft.epage=1654&rft.pages=1653-1654&rft.issn=1755-4330&rft.eissn=1755-4349&rft_id=info:doi/10.1038/s41557-023-01369-w&rft_dat=%3Cproquest_cross%3E2896809103%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=2897542071&rft_id=info:pmid/&rfr_iscdi=true