Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient...
Gespeichert in:
| Veröffentlicht in: | Physical chemistry chemical physics : PCCP 2016-02, Vol.18 (8), p.572-576 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 576 |
|---|---|
| container_issue | 8 |
| container_start_page | 572 |
| container_title | Physical chemistry chemical physics : PCCP |
| container_volume | 18 |
| creator | Rossetti, G Musiani, F Abad, E Dibenedetto, D Mouhib, H Fernandez, C. O Carloni, P |
| description | We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Enhanced sampling simulations of N-terminally acetylated human α-synuclein suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix altering protein dynamics at the N-terminal and intramolecular interactions. |
| doi_str_mv | 10.1039/c5cp04549e |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_26553504</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1793262555</sourcerecordid><originalsourceid>FETCH-LOGICAL-c419t-5c3de225d960cbe873ef291f80b76caea5d6786502f205b472ee8d32e30125b63</originalsourceid><addsrcrecordid>eNqF0ctKxDAUBuAgiqOjG_dKliJUc2-7lDJeYEAXui5peupU0qYm7aKP5Yv4THaccVy6OoF8-SH_QeiMkmtKeHpjpOmIkCKFPXREheJRShKxvzvHaoaOQ3gnhFBJ-SGaMSUll0QcIZO5tnK-0X3tWm0xtAGawgJ2FV4NjW7x12cUxnYwFuoWd6sx1M66t9pMeP0Qdx7K2vRQ4mLEjbNgBqs9DnUzzXVqOEEHlbYBTrdzjl7vFi_ZQ7R8un_MbpeRETTtI2l4CYzJMlXEFJDEHCqW0iohRayMBi1LFSdKElYxIgsRM4Ck5Aw4oUwWis_R5Sa38-5jgNDnTR0MWKtbcEPIaZxyppic_v4_VYqpmDIx0asNNd6F4KHKO1832o85Jfm6_zyT2fNP_4sJX2xzh6KBckd_C5_A-Qb4YHa3fwvk37Q3i_s</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1766267124</pqid></control><display><type>article</type><title>Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Rossetti, G ; Musiani, F ; Abad, E ; Dibenedetto, D ; Mouhib, H ; Fernandez, C. O ; Carloni, P</creator><creatorcontrib>Rossetti, G ; Musiani, F ; Abad, E ; Dibenedetto, D ; Mouhib, H ; Fernandez, C. O ; Carloni, P</creatorcontrib><description>We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Enhanced sampling simulations of N-terminally acetylated human α-synuclein suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix altering protein dynamics at the N-terminal and intramolecular interactions.</description><identifier>ISSN: 1463-9076</identifier><identifier>EISSN: 1463-9084</identifier><identifier>DOI: 10.1039/c5cp04549e</identifier><identifier>PMID: 26553504</identifier><language>eng</language><publisher>England</publisher><subject>Acetylation ; alpha-Synuclein - chemistry ; alpha-Synuclein - metabolism ; Circular Dichroism ; Dynamics ; Human ; Human performance ; Humans ; Mathematical analysis ; Molecular Conformation ; Molecular Dynamics Simulation ; Parkinson Disease - physiopathology ; Physical chemistry ; Protein Processing, Post-Translational ; Proteins ; Sampling ; Simulation</subject><ispartof>Physical chemistry chemical physics : PCCP, 2016-02, Vol.18 (8), p.572-576</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c419t-5c3de225d960cbe873ef291f80b76caea5d6786502f205b472ee8d32e30125b63</citedby><cites>FETCH-LOGICAL-c419t-5c3de225d960cbe873ef291f80b76caea5d6786502f205b472ee8d32e30125b63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26553504$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rossetti, G</creatorcontrib><creatorcontrib>Musiani, F</creatorcontrib><creatorcontrib>Abad, E</creatorcontrib><creatorcontrib>Dibenedetto, D</creatorcontrib><creatorcontrib>Mouhib, H</creatorcontrib><creatorcontrib>Fernandez, C. O</creatorcontrib><creatorcontrib>Carloni, P</creatorcontrib><title>Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations</title><title>Physical chemistry chemical physics : PCCP</title><addtitle>Phys Chem Chem Phys</addtitle><description>We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Enhanced sampling simulations of N-terminally acetylated human α-synuclein suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix altering protein dynamics at the N-terminal and intramolecular interactions.</description><subject>Acetylation</subject><subject>alpha-Synuclein - chemistry</subject><subject>alpha-Synuclein - metabolism</subject><subject>Circular Dichroism</subject><subject>Dynamics</subject><subject>Human</subject><subject>Human performance</subject><subject>Humans</subject><subject>Mathematical analysis</subject><subject>Molecular Conformation</subject><subject>Molecular Dynamics Simulation</subject><subject>Parkinson Disease - physiopathology</subject><subject>Physical chemistry</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Sampling</subject><subject>Simulation</subject><issn>1463-9076</issn><issn>1463-9084</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0ctKxDAUBuAgiqOjG_dKliJUc2-7lDJeYEAXui5peupU0qYm7aKP5Yv4THaccVy6OoF8-SH_QeiMkmtKeHpjpOmIkCKFPXREheJRShKxvzvHaoaOQ3gnhFBJ-SGaMSUll0QcIZO5tnK-0X3tWm0xtAGawgJ2FV4NjW7x12cUxnYwFuoWd6sx1M66t9pMeP0Qdx7K2vRQ4mLEjbNgBqs9DnUzzXVqOEEHlbYBTrdzjl7vFi_ZQ7R8un_MbpeRETTtI2l4CYzJMlXEFJDEHCqW0iohRayMBi1LFSdKElYxIgsRM4Ck5Aw4oUwWis_R5Sa38-5jgNDnTR0MWKtbcEPIaZxyppic_v4_VYqpmDIx0asNNd6F4KHKO1832o85Jfm6_zyT2fNP_4sJX2xzh6KBckd_C5_A-Qb4YHa3fwvk37Q3i_s</recordid><startdate>20160217</startdate><enddate>20160217</enddate><creator>Rossetti, G</creator><creator>Musiani, F</creator><creator>Abad, E</creator><creator>Dibenedetto, D</creator><creator>Mouhib, H</creator><creator>Fernandez, C. O</creator><creator>Carloni, P</creator><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>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20160217</creationdate><title>Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations</title><author>Rossetti, G ; Musiani, F ; Abad, E ; Dibenedetto, D ; Mouhib, H ; Fernandez, C. O ; Carloni, P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c419t-5c3de225d960cbe873ef291f80b76caea5d6786502f205b472ee8d32e30125b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Acetylation</topic><topic>alpha-Synuclein - chemistry</topic><topic>alpha-Synuclein - metabolism</topic><topic>Circular Dichroism</topic><topic>Dynamics</topic><topic>Human</topic><topic>Human performance</topic><topic>Humans</topic><topic>Mathematical analysis</topic><topic>Molecular Conformation</topic><topic>Molecular Dynamics Simulation</topic><topic>Parkinson Disease - physiopathology</topic><topic>Physical chemistry</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Sampling</topic><topic>Simulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rossetti, G</creatorcontrib><creatorcontrib>Musiani, F</creatorcontrib><creatorcontrib>Abad, E</creatorcontrib><creatorcontrib>Dibenedetto, D</creatorcontrib><creatorcontrib>Mouhib, H</creatorcontrib><creatorcontrib>Fernandez, C. O</creatorcontrib><creatorcontrib>Carloni, P</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><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Physical chemistry chemical physics : PCCP</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rossetti, G</au><au>Musiani, F</au><au>Abad, E</au><au>Dibenedetto, D</au><au>Mouhib, H</au><au>Fernandez, C. O</au><au>Carloni, P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations</atitle><jtitle>Physical chemistry chemical physics : PCCP</jtitle><addtitle>Phys Chem Chem Phys</addtitle><date>2016-02-17</date><risdate>2016</risdate><volume>18</volume><issue>8</issue><spage>572</spage><epage>576</epage><pages>572-576</pages><issn>1463-9076</issn><eissn>1463-9084</eissn><abstract>We perform here enhanced sampling simulations of N-terminally acetylated human α-synuclein, an intrinsically disordered protein involved in Parkinson's disease. The calculations, consistent with experiments, suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix. The latter, absent in the non-physiological form, alters protein dynamics at the N-terminal and intramolecular interactions.
Enhanced sampling simulations of N-terminally acetylated human α-synuclein suggest that the post-translational modification leads to the formation of a transient amphipathic α-helix altering protein dynamics at the N-terminal and intramolecular interactions.</abstract><cop>England</cop><pmid>26553504</pmid><doi>10.1039/c5cp04549e</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1463-9076 |
| ispartof | Physical chemistry chemical physics : PCCP, 2016-02, Vol.18 (8), p.572-576 |
| issn | 1463-9076 1463-9084 |
| language | eng |
| recordid | cdi_pubmed_primary_26553504 |
| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Acetylation alpha-Synuclein - chemistry alpha-Synuclein - metabolism Circular Dichroism Dynamics Human Human performance Humans Mathematical analysis Molecular Conformation Molecular Dynamics Simulation Parkinson Disease - physiopathology Physical chemistry Protein Processing, Post-Translational Proteins Sampling Simulation |
| title | Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-24T11%3A05%3A38IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Conformational%20ensemble%20of%20human%20%CE%B1-synuclein%20physiological%20form%20predicted%20by%20molecular%20simulations&rft.jtitle=Physical%20chemistry%20chemical%20physics%20:%20PCCP&rft.au=Rossetti,%20G&rft.date=2016-02-17&rft.volume=18&rft.issue=8&rft.spage=572&rft.epage=576&rft.pages=572-576&rft.issn=1463-9076&rft.eissn=1463-9084&rft_id=info:doi/10.1039/c5cp04549e&rft_dat=%3Cproquest_pubme%3E1793262555%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1766267124&rft_id=info:pmid/26553504&rfr_iscdi=true |