Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning
Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic‐angle‐spinning (MAS) NMR experiments. However, the resolution of the DNP NMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryog...
Gespeichert in:
| Veröffentlicht in: | Angewandte Chemie International Edition 2018-06, Vol.57 (25), p.7458-7462 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 7462 |
|---|---|
| container_issue | 25 |
| container_start_page | 7458 |
| container_title | Angewandte Chemie International Edition |
| container_volume | 57 |
| creator | Jaudzems, Kristaps Bertarello, Andrea Chaudhari, Sachin R. Pica, Andrea Cala‐De Paepe, Diane Barbet‐Massin, Emeline Pell, Andrew J. Akopjana, Inara Kotelovica, Svetlana Gajan, David Ouari, Olivier Tars, Kaspars Pintacuda, Guido Lesage, Anne |
| description | Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic‐angle‐spinning (MAS) NMR experiments. However, the resolution of the DNP NMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryogenic temperatures and in the presence of paramagnetic radicals. High‐quality DNP‐enhanced NMR spectra of the Acinetobacter phage 205 (AP205) nucleocapsid can be obtained by combining high magnetic field (800 MHz) and fast MAS (40 kHz). These conditions yield enhanced resolution and long coherence lifetimes allowing the acquisition of resolved 2D correlation spectra and of previously unfeasible scalar‐based experiments. This enables the assignment of aromatic resonances of the AP205 coat protein and its packaged RNA, as well as the detection of long‐range contacts, which are not observed at room temperature, opening new possibilities for structure determination.
Restored resolution: With 40 kHz magic‐angle‐spinning probes, the resolution in the dynamic nuclear polarization‐enhanced solid‐state NMR spectra of biomolecules acquired at 115 K and 800 MHz is significantly improved. Together with increased coherence lifetimes, this allows site‐specific assignment of aromatic and nucleic acid resonances and of long‐range contacts in a nucleocapsid by joint analysis of dipolar and through‐bond correlations. |
| doi_str_mv | 10.1002/anie.201801016 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_01859534v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2053266871</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4446-fe49a8342cba13e52123bcbf4ca15db4bdd5de0405942219613d857ce31c91ad3</originalsourceid><addsrcrecordid>eNqFkcuO0zAUhiMEYoaBLUtkiQ0sUnxN7GUZWjpSpyAua8txTluPHLvkwqhISDwCz8iT4ChDkdiwsuXznU8-58-ypwTPCMb0lQkOZhQTiQkmxb3snAhKclaW7H66c8byUgpylj3qupvES4mLh9kZVaIoqFLn2fc3x2AaZ9FmsB5Mi95Hb1r3zfQuhl8_fi7C3gQLNXrtYhM92CGV0eb6A_p4ANu3sbPxcESmRyu326NrswvQJ93Sga_Rrev3aGm6fiw4m3zzsPOQel0ILuweZw-2xnfw5O68yD4vF58uV_n63dury_k6t5zzIt8CV0YyTm1lCIM0IWWVrbbcGiLqild1LWrAHAvFKSWqIKyWorTAiFXE1Owiezl598brQ-sa0x51NE6v5ms9vqUFCiUY_0oS-2JiD238MkDX68Z1Frw3AeLQ6WnZUnKZ0Of_oDdxaEOaJFGC0aKQ5SicTZRN2-pa2J5-QLAeQ9RjiPoUYmp4dqcdqgbqE_4ntQSoCbh1Ho7_0en55mrxV_4bupep4A</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2053266871</pqid></control><display><type>article</type><title>Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning</title><source>Wiley Online Library Journals Frontfile Complete</source><creator>Jaudzems, Kristaps ; Bertarello, Andrea ; Chaudhari, Sachin R. ; Pica, Andrea ; Cala‐De Paepe, Diane ; Barbet‐Massin, Emeline ; Pell, Andrew J. ; Akopjana, Inara ; Kotelovica, Svetlana ; Gajan, David ; Ouari, Olivier ; Tars, Kaspars ; Pintacuda, Guido ; Lesage, Anne</creator><creatorcontrib>Jaudzems, Kristaps ; Bertarello, Andrea ; Chaudhari, Sachin R. ; Pica, Andrea ; Cala‐De Paepe, Diane ; Barbet‐Massin, Emeline ; Pell, Andrew J. ; Akopjana, Inara ; Kotelovica, Svetlana ; Gajan, David ; Ouari, Olivier ; Tars, Kaspars ; Pintacuda, Guido ; Lesage, Anne</creatorcontrib><description>Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic‐angle‐spinning (MAS) NMR experiments. However, the resolution of the DNP NMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryogenic temperatures and in the presence of paramagnetic radicals. High‐quality DNP‐enhanced NMR spectra of the Acinetobacter phage 205 (AP205) nucleocapsid can be obtained by combining high magnetic field (800 MHz) and fast MAS (40 kHz). These conditions yield enhanced resolution and long coherence lifetimes allowing the acquisition of resolved 2D correlation spectra and of previously unfeasible scalar‐based experiments. This enables the assignment of aromatic resonances of the AP205 coat protein and its packaged RNA, as well as the detection of long‐range contacts, which are not observed at room temperature, opening new possibilities for structure determination.
Restored resolution: With 40 kHz magic‐angle‐spinning probes, the resolution in the dynamic nuclear polarization‐enhanced solid‐state NMR spectra of biomolecules acquired at 115 K and 800 MHz is significantly improved. Together with increased coherence lifetimes, this allows site‐specific assignment of aromatic and nucleic acid resonances and of long‐range contacts in a nucleocapsid by joint analysis of dipolar and through‐bond correlations.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201801016</identifier><identifier>PMID: 29566299</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>biomolecular NMR ; Chemical Sciences ; Coat protein ; Cryogenic temperature ; dynamic nuclear polarization ; Experiments ; Line broadening ; magic-angle spinning ; Magnetic fields ; Magnetic resonance spectroscopy ; NMR spectroscopy ; Nucleocapsids ; Phages ; Polarization ; Proteins ; Ribonucleic acid ; RNA ; Signal to noise ratio ; solid-state NMR spectroscopy ; Spectra ; Spectrum analysis</subject><ispartof>Angewandte Chemie International Edition, 2018-06, Vol.57 (25), p.7458-7462</ispartof><rights>2018 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4446-fe49a8342cba13e52123bcbf4ca15db4bdd5de0405942219613d857ce31c91ad3</citedby><cites>FETCH-LOGICAL-c4446-fe49a8342cba13e52123bcbf4ca15db4bdd5de0405942219613d857ce31c91ad3</cites><orcidid>0000-0003-1958-2840 ; 0000-0001-7757-2144 ; 0000-0002-0182-1674 ; 0000-0002-8736-8742 ; 0000-0003-3705-1760</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fanie.201801016$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.201801016$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,776,780,881,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29566299$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01859534$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Jaudzems, Kristaps</creatorcontrib><creatorcontrib>Bertarello, Andrea</creatorcontrib><creatorcontrib>Chaudhari, Sachin R.</creatorcontrib><creatorcontrib>Pica, Andrea</creatorcontrib><creatorcontrib>Cala‐De Paepe, Diane</creatorcontrib><creatorcontrib>Barbet‐Massin, Emeline</creatorcontrib><creatorcontrib>Pell, Andrew J.</creatorcontrib><creatorcontrib>Akopjana, Inara</creatorcontrib><creatorcontrib>Kotelovica, Svetlana</creatorcontrib><creatorcontrib>Gajan, David</creatorcontrib><creatorcontrib>Ouari, Olivier</creatorcontrib><creatorcontrib>Tars, Kaspars</creatorcontrib><creatorcontrib>Pintacuda, Guido</creatorcontrib><creatorcontrib>Lesage, Anne</creatorcontrib><title>Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic‐angle‐spinning (MAS) NMR experiments. However, the resolution of the DNP NMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryogenic temperatures and in the presence of paramagnetic radicals. High‐quality DNP‐enhanced NMR spectra of the Acinetobacter phage 205 (AP205) nucleocapsid can be obtained by combining high magnetic field (800 MHz) and fast MAS (40 kHz). These conditions yield enhanced resolution and long coherence lifetimes allowing the acquisition of resolved 2D correlation spectra and of previously unfeasible scalar‐based experiments. This enables the assignment of aromatic resonances of the AP205 coat protein and its packaged RNA, as well as the detection of long‐range contacts, which are not observed at room temperature, opening new possibilities for structure determination.
Restored resolution: With 40 kHz magic‐angle‐spinning probes, the resolution in the dynamic nuclear polarization‐enhanced solid‐state NMR spectra of biomolecules acquired at 115 K and 800 MHz is significantly improved. Together with increased coherence lifetimes, this allows site‐specific assignment of aromatic and nucleic acid resonances and of long‐range contacts in a nucleocapsid by joint analysis of dipolar and through‐bond correlations.</description><subject>biomolecular NMR</subject><subject>Chemical Sciences</subject><subject>Coat protein</subject><subject>Cryogenic temperature</subject><subject>dynamic nuclear polarization</subject><subject>Experiments</subject><subject>Line broadening</subject><subject>magic-angle spinning</subject><subject>Magnetic fields</subject><subject>Magnetic resonance spectroscopy</subject><subject>NMR spectroscopy</subject><subject>Nucleocapsids</subject><subject>Phages</subject><subject>Polarization</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Signal to noise ratio</subject><subject>solid-state NMR spectroscopy</subject><subject>Spectra</subject><subject>Spectrum analysis</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFkcuO0zAUhiMEYoaBLUtkiQ0sUnxN7GUZWjpSpyAua8txTluPHLvkwqhISDwCz8iT4ChDkdiwsuXznU8-58-ypwTPCMb0lQkOZhQTiQkmxb3snAhKclaW7H66c8byUgpylj3qupvES4mLh9kZVaIoqFLn2fc3x2AaZ9FmsB5Mi95Hb1r3zfQuhl8_fi7C3gQLNXrtYhM92CGV0eb6A_p4ANu3sbPxcESmRyu326NrswvQJ93Sga_Rrev3aGm6fiw4m3zzsPOQel0ILuweZw-2xnfw5O68yD4vF58uV_n63dury_k6t5zzIt8CV0YyTm1lCIM0IWWVrbbcGiLqild1LWrAHAvFKSWqIKyWorTAiFXE1Owiezl598brQ-sa0x51NE6v5ms9vqUFCiUY_0oS-2JiD238MkDX68Z1Frw3AeLQ6WnZUnKZ0Of_oDdxaEOaJFGC0aKQ5SicTZRN2-pa2J5-QLAeQ9RjiPoUYmp4dqcdqgbqE_4ntQSoCbh1Ho7_0en55mrxV_4bupep4A</recordid><startdate>20180618</startdate><enddate>20180618</enddate><creator>Jaudzems, Kristaps</creator><creator>Bertarello, Andrea</creator><creator>Chaudhari, Sachin R.</creator><creator>Pica, Andrea</creator><creator>Cala‐De Paepe, Diane</creator><creator>Barbet‐Massin, Emeline</creator><creator>Pell, Andrew J.</creator><creator>Akopjana, Inara</creator><creator>Kotelovica, Svetlana</creator><creator>Gajan, David</creator><creator>Ouari, Olivier</creator><creator>Tars, Kaspars</creator><creator>Pintacuda, Guido</creator><creator>Lesage, Anne</creator><general>Wiley Subscription Services, Inc</general><general>Wiley-VCH Verlag</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>K9.</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-1958-2840</orcidid><orcidid>https://orcid.org/0000-0001-7757-2144</orcidid><orcidid>https://orcid.org/0000-0002-0182-1674</orcidid><orcidid>https://orcid.org/0000-0002-8736-8742</orcidid><orcidid>https://orcid.org/0000-0003-3705-1760</orcidid></search><sort><creationdate>20180618</creationdate><title>Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning</title><author>Jaudzems, Kristaps ; Bertarello, Andrea ; Chaudhari, Sachin R. ; Pica, Andrea ; Cala‐De Paepe, Diane ; Barbet‐Massin, Emeline ; Pell, Andrew J. ; Akopjana, Inara ; Kotelovica, Svetlana ; Gajan, David ; Ouari, Olivier ; Tars, Kaspars ; Pintacuda, Guido ; Lesage, Anne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4446-fe49a8342cba13e52123bcbf4ca15db4bdd5de0405942219613d857ce31c91ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>biomolecular NMR</topic><topic>Chemical Sciences</topic><topic>Coat protein</topic><topic>Cryogenic temperature</topic><topic>dynamic nuclear polarization</topic><topic>Experiments</topic><topic>Line broadening</topic><topic>magic-angle spinning</topic><topic>Magnetic fields</topic><topic>Magnetic resonance spectroscopy</topic><topic>NMR spectroscopy</topic><topic>Nucleocapsids</topic><topic>Phages</topic><topic>Polarization</topic><topic>Proteins</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>Signal to noise ratio</topic><topic>solid-state NMR spectroscopy</topic><topic>Spectra</topic><topic>Spectrum analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jaudzems, Kristaps</creatorcontrib><creatorcontrib>Bertarello, Andrea</creatorcontrib><creatorcontrib>Chaudhari, Sachin R.</creatorcontrib><creatorcontrib>Pica, Andrea</creatorcontrib><creatorcontrib>Cala‐De Paepe, Diane</creatorcontrib><creatorcontrib>Barbet‐Massin, Emeline</creatorcontrib><creatorcontrib>Pell, Andrew J.</creatorcontrib><creatorcontrib>Akopjana, Inara</creatorcontrib><creatorcontrib>Kotelovica, Svetlana</creatorcontrib><creatorcontrib>Gajan, David</creatorcontrib><creatorcontrib>Ouari, Olivier</creatorcontrib><creatorcontrib>Tars, Kaspars</creatorcontrib><creatorcontrib>Pintacuda, Guido</creatorcontrib><creatorcontrib>Lesage, Anne</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jaudzems, Kristaps</au><au>Bertarello, Andrea</au><au>Chaudhari, Sachin R.</au><au>Pica, Andrea</au><au>Cala‐De Paepe, Diane</au><au>Barbet‐Massin, Emeline</au><au>Pell, Andrew J.</au><au>Akopjana, Inara</au><au>Kotelovica, Svetlana</au><au>Gajan, David</au><au>Ouari, Olivier</au><au>Tars, Kaspars</au><au>Pintacuda, Guido</au><au>Lesage, Anne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2018-06-18</date><risdate>2018</risdate><volume>57</volume><issue>25</issue><spage>7458</spage><epage>7462</epage><pages>7458-7462</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>Dynamic nuclear polarization (DNP) is a powerful way to overcome the sensitivity limitation of magic‐angle‐spinning (MAS) NMR experiments. However, the resolution of the DNP NMR spectra of proteins is compromised by severe line broadening associated with the necessity to perform experiments at cryogenic temperatures and in the presence of paramagnetic radicals. High‐quality DNP‐enhanced NMR spectra of the Acinetobacter phage 205 (AP205) nucleocapsid can be obtained by combining high magnetic field (800 MHz) and fast MAS (40 kHz). These conditions yield enhanced resolution and long coherence lifetimes allowing the acquisition of resolved 2D correlation spectra and of previously unfeasible scalar‐based experiments. This enables the assignment of aromatic resonances of the AP205 coat protein and its packaged RNA, as well as the detection of long‐range contacts, which are not observed at room temperature, opening new possibilities for structure determination.
Restored resolution: With 40 kHz magic‐angle‐spinning probes, the resolution in the dynamic nuclear polarization‐enhanced solid‐state NMR spectra of biomolecules acquired at 115 K and 800 MHz is significantly improved. Together with increased coherence lifetimes, this allows site‐specific assignment of aromatic and nucleic acid resonances and of long‐range contacts in a nucleocapsid by joint analysis of dipolar and through‐bond correlations.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29566299</pmid><doi>10.1002/anie.201801016</doi><tpages>5</tpages><edition>International ed. in English</edition><orcidid>https://orcid.org/0000-0003-1958-2840</orcidid><orcidid>https://orcid.org/0000-0001-7757-2144</orcidid><orcidid>https://orcid.org/0000-0002-0182-1674</orcidid><orcidid>https://orcid.org/0000-0002-8736-8742</orcidid><orcidid>https://orcid.org/0000-0003-3705-1760</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1433-7851 |
| ispartof | Angewandte Chemie International Edition, 2018-06, Vol.57 (25), p.7458-7462 |
| issn | 1433-7851 1521-3773 |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_01859534v1 |
| source | Wiley Online Library Journals Frontfile Complete |
| subjects | biomolecular NMR Chemical Sciences Coat protein Cryogenic temperature dynamic nuclear polarization Experiments Line broadening magic-angle spinning Magnetic fields Magnetic resonance spectroscopy NMR spectroscopy Nucleocapsids Phages Polarization Proteins Ribonucleic acid RNA Signal to noise ratio solid-state NMR spectroscopy Spectra Spectrum analysis |
| title | Dynamic Nuclear Polarization‐Enhanced Biomolecular NMR Spectroscopy at High Magnetic Field with Fast Magic‐Angle Spinning |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-09T09%3A48%3A02IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Dynamic%20Nuclear%20Polarization%E2%80%90Enhanced%20Biomolecular%20NMR%20Spectroscopy%20at%20High%20Magnetic%20Field%20with%20Fast%20Magic%E2%80%90Angle%20Spinning&rft.jtitle=Angewandte%20Chemie%20International%20Edition&rft.au=Jaudzems,%20Kristaps&rft.date=2018-06-18&rft.volume=57&rft.issue=25&rft.spage=7458&rft.epage=7462&rft.pages=7458-7462&rft.issn=1433-7851&rft.eissn=1521-3773&rft_id=info:doi/10.1002/anie.201801016&rft_dat=%3Cproquest_hal_p%3E2053266871%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2053266871&rft_id=info:pmid/29566299&rfr_iscdi=true |