Multiscale simulations of large complexes in conjunction with cryo-EM analysis
The cellular environment is highly crowded with most proteins and RNA/DNA forming homomeric and heteromeric complexes. Essential questions regarding how these complexes switch between functional, rest, and abnormal states with regulators or modifications remain challenging and complicated. Here, we...
Gespeichert in:
| Veröffentlicht in: | Current opinion in structural biology 2022-02, Vol.72, p.27-32 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 32 |
|---|---|
| container_issue | |
| container_start_page | 27 |
| container_title | Current opinion in structural biology |
| container_volume | 72 |
| creator | Liao, Chenyi Liu, Ye Zhang, Dinglin Li, Guohui |
| description | The cellular environment is highly crowded with most proteins and RNA/DNA forming homomeric and heteromeric complexes. Essential questions regarding how these complexes switch between functional, rest, and abnormal states with regulators or modifications remain challenging and complicated. Here, we review the recent progress integrating cryoelectron microscopy and multiscale molecular modeling to understand the dynamics and function-related mechanism in protein–RNA/DNA complexes, protein–protein complexes/assemblies, and membrane protein complexes. One future direction of multiscale simulations will be to interpret the large complex multibody regulation in assembly-induced function enhancement in conjunction with advanced atomic resolution structural-biology techniques and specialized computing architectures.
[Display omitted] |
| doi_str_mv | 10.1016/j.sbi.2021.07.008 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2562235796</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0959440X2100110X</els_id><sourcerecordid>2562235796</sourcerecordid><originalsourceid>FETCH-LOGICAL-c353t-b4de5491f2225e6b15124581d267d500638061f214f59bc251b26a743e2b34d43</originalsourceid><addsrcrecordid>eNp9kMtOwzAQRS0EoqXwAWxQlmwS_MxDrFBVHhKFDUjdWY4zAUdOUuwE6N_jqoUlq9FI517NHITOCU4IJulVk_jSJBRTkuAswTg_QFOSZ0WMGVsdoikuRBFzjlcTdOJ9gzFOCc-P0YRxVhREiCl6Wo52MF4rC5E37WjVYPrOR30dWeXeINJ9u7bwDT4yXVi6Zuz0Fom-zPAeabfp48UyUp2yG2_8KTqqlfVwtp8z9Hq7eJnfx4_Pdw_zm8dYM8GGuOQVCF6QmlIqIC2JIJSLnFQ0zSoRzmR5OLWmhNeiKDUVpKSpyjgDWjJecTZDl7vetes_RvCDbMMTYK3qoB-9pCKllImsSANKdqh2vfcOarl2plVuIwmWW42ykUGj3GqUOJNBY8hc7OvHsoXqL_HrLQDXOwDCk58GnPTaQKehMg70IKve_FP_A3b_gho</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2562235796</pqid></control><display><type>article</type><title>Multiscale simulations of large complexes in conjunction with cryo-EM analysis</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Liao, Chenyi ; Liu, Ye ; Zhang, Dinglin ; Li, Guohui</creator><creatorcontrib>Liao, Chenyi ; Liu, Ye ; Zhang, Dinglin ; Li, Guohui</creatorcontrib><description>The cellular environment is highly crowded with most proteins and RNA/DNA forming homomeric and heteromeric complexes. Essential questions regarding how these complexes switch between functional, rest, and abnormal states with regulators or modifications remain challenging and complicated. Here, we review the recent progress integrating cryoelectron microscopy and multiscale molecular modeling to understand the dynamics and function-related mechanism in protein–RNA/DNA complexes, protein–protein complexes/assemblies, and membrane protein complexes. One future direction of multiscale simulations will be to interpret the large complex multibody regulation in assembly-induced function enhancement in conjunction with advanced atomic resolution structural-biology techniques and specialized computing architectures.
[Display omitted]</description><identifier>ISSN: 0959-440X</identifier><identifier>EISSN: 1879-033X</identifier><identifier>DOI: 10.1016/j.sbi.2021.07.008</identifier><identifier>PMID: 34399155</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Cryoelectron microscopy ; Cryoelectron Microscopy - methods ; DNA ; Membrane protein complex ; Models, Molecular ; Multiscale modeling ; Proteins ; Protein–protein complex ; Protein–RNA/DNA complex ; RNA</subject><ispartof>Current opinion in structural biology, 2022-02, Vol.72, p.27-32</ispartof><rights>2021 Elsevier Ltd</rights><rights>Copyright © 2021 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-b4de5491f2225e6b15124581d267d500638061f214f59bc251b26a743e2b34d43</citedby><cites>FETCH-LOGICAL-c353t-b4de5491f2225e6b15124581d267d500638061f214f59bc251b26a743e2b34d43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0959440X2100110X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34399155$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liao, Chenyi</creatorcontrib><creatorcontrib>Liu, Ye</creatorcontrib><creatorcontrib>Zhang, Dinglin</creatorcontrib><creatorcontrib>Li, Guohui</creatorcontrib><title>Multiscale simulations of large complexes in conjunction with cryo-EM analysis</title><title>Current opinion in structural biology</title><addtitle>Curr Opin Struct Biol</addtitle><description>The cellular environment is highly crowded with most proteins and RNA/DNA forming homomeric and heteromeric complexes. Essential questions regarding how these complexes switch between functional, rest, and abnormal states with regulators or modifications remain challenging and complicated. Here, we review the recent progress integrating cryoelectron microscopy and multiscale molecular modeling to understand the dynamics and function-related mechanism in protein–RNA/DNA complexes, protein–protein complexes/assemblies, and membrane protein complexes. One future direction of multiscale simulations will be to interpret the large complex multibody regulation in assembly-induced function enhancement in conjunction with advanced atomic resolution structural-biology techniques and specialized computing architectures.
[Display omitted]</description><subject>Cryoelectron microscopy</subject><subject>Cryoelectron Microscopy - methods</subject><subject>DNA</subject><subject>Membrane protein complex</subject><subject>Models, Molecular</subject><subject>Multiscale modeling</subject><subject>Proteins</subject><subject>Protein–protein complex</subject><subject>Protein–RNA/DNA complex</subject><subject>RNA</subject><issn>0959-440X</issn><issn>1879-033X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS0EoqXwAWxQlmwS_MxDrFBVHhKFDUjdWY4zAUdOUuwE6N_jqoUlq9FI517NHITOCU4IJulVk_jSJBRTkuAswTg_QFOSZ0WMGVsdoikuRBFzjlcTdOJ9gzFOCc-P0YRxVhREiCl6Wo52MF4rC5E37WjVYPrOR30dWeXeINJ9u7bwDT4yXVi6Zuz0Fom-zPAeabfp48UyUp2yG2_8KTqqlfVwtp8z9Hq7eJnfx4_Pdw_zm8dYM8GGuOQVCF6QmlIqIC2JIJSLnFQ0zSoRzmR5OLWmhNeiKDUVpKSpyjgDWjJecTZDl7vetes_RvCDbMMTYK3qoB-9pCKllImsSANKdqh2vfcOarl2plVuIwmWW42ykUGj3GqUOJNBY8hc7OvHsoXqL_HrLQDXOwDCk58GnPTaQKehMg70IKve_FP_A3b_gho</recordid><startdate>202202</startdate><enddate>202202</enddate><creator>Liao, Chenyi</creator><creator>Liu, Ye</creator><creator>Zhang, Dinglin</creator><creator>Li, Guohui</creator><general>Elsevier Ltd</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></search><sort><creationdate>202202</creationdate><title>Multiscale simulations of large complexes in conjunction with cryo-EM analysis</title><author>Liao, Chenyi ; Liu, Ye ; Zhang, Dinglin ; Li, Guohui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-b4de5491f2225e6b15124581d267d500638061f214f59bc251b26a743e2b34d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Cryoelectron microscopy</topic><topic>Cryoelectron Microscopy - methods</topic><topic>DNA</topic><topic>Membrane protein complex</topic><topic>Models, Molecular</topic><topic>Multiscale modeling</topic><topic>Proteins</topic><topic>Protein–protein complex</topic><topic>Protein–RNA/DNA complex</topic><topic>RNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liao, Chenyi</creatorcontrib><creatorcontrib>Liu, Ye</creatorcontrib><creatorcontrib>Zhang, Dinglin</creatorcontrib><creatorcontrib>Li, Guohui</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><jtitle>Current opinion in structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liao, Chenyi</au><au>Liu, Ye</au><au>Zhang, Dinglin</au><au>Li, Guohui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multiscale simulations of large complexes in conjunction with cryo-EM analysis</atitle><jtitle>Current opinion in structural biology</jtitle><addtitle>Curr Opin Struct Biol</addtitle><date>2022-02</date><risdate>2022</risdate><volume>72</volume><spage>27</spage><epage>32</epage><pages>27-32</pages><issn>0959-440X</issn><eissn>1879-033X</eissn><abstract>The cellular environment is highly crowded with most proteins and RNA/DNA forming homomeric and heteromeric complexes. Essential questions regarding how these complexes switch between functional, rest, and abnormal states with regulators or modifications remain challenging and complicated. Here, we review the recent progress integrating cryoelectron microscopy and multiscale molecular modeling to understand the dynamics and function-related mechanism in protein–RNA/DNA complexes, protein–protein complexes/assemblies, and membrane protein complexes. One future direction of multiscale simulations will be to interpret the large complex multibody regulation in assembly-induced function enhancement in conjunction with advanced atomic resolution structural-biology techniques and specialized computing architectures.
[Display omitted]</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>34399155</pmid><doi>10.1016/j.sbi.2021.07.008</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0959-440X |
| ispartof | Current opinion in structural biology, 2022-02, Vol.72, p.27-32 |
| issn | 0959-440X 1879-033X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2562235796 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Cryoelectron microscopy Cryoelectron Microscopy - methods DNA Membrane protein complex Models, Molecular Multiscale modeling Proteins Protein–protein complex Protein–RNA/DNA complex RNA |
| title | Multiscale simulations of large complexes in conjunction with cryo-EM analysis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T09%3A54%3A05IST&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=Multiscale%20simulations%20of%20large%20complexes%20in%20conjunction%20with%20cryo-EM%20analysis&rft.jtitle=Current%20opinion%20in%20structural%20biology&rft.au=Liao,%20Chenyi&rft.date=2022-02&rft.volume=72&rft.spage=27&rft.epage=32&rft.pages=27-32&rft.issn=0959-440X&rft.eissn=1879-033X&rft_id=info:doi/10.1016/j.sbi.2021.07.008&rft_dat=%3Cproquest_cross%3E2562235796%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=2562235796&rft_id=info:pmid/34399155&rft_els_id=S0959440X2100110X&rfr_iscdi=true |