Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR
[Display omitted] •We apply the RelaX-EXSY method to measure H/D exchange in a solid state protein.•The method requires proton detection and performs better at higher external magnetic fields.•Amide exchange rates are measured in deuterated Salmonella typhimurium type iii secretion system (T3SS) nee...
Gespeichert in:
| Veröffentlicht in: | Journal of magnetic resonance (1997) 2017-10, Vol.283, p.110-116 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 116 |
|---|---|
| container_issue | |
| container_start_page | 110 |
| container_title | Journal of magnetic resonance (1997) |
| container_volume | 283 |
| creator | Chevelkov, Veniamin Giller, Karin Becker, Stefan Lange, Adam |
| description | [Display omitted]
•We apply the RelaX-EXSY method to measure H/D exchange in a solid state protein.•The method requires proton detection and performs better at higher external magnetic fields.•Amide exchange rates are measured in deuterated Salmonella typhimurium type iii secretion system (T3SS) needles.
In this report we present site-specific measurements of amide hydrogen-deuterium exchange rates in a protein in the solid state phase by MAS NMR. Employing perdeuteration, proton detection and a high external magnetic field we could adopt the highly efficient Relax-EXSY protocol previously developed for liquid state NMR. According to this method, we measured the contribution of hydrogen exchange on apparent 15N longitudinal relaxation rates in samples with differing D2O buffer content. Differences in the apparent T1 times allowed us to derive exchange rates for multiple residues in the type III secretion system needle protein. |
| doi_str_mv | 10.1016/j.jmr.2017.08.012 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1948759730</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1090780717302203</els_id><sourcerecordid>1948759730</sourcerecordid><originalsourceid>FETCH-LOGICAL-e263t-aa4854bdd6ffdfed9c4354deff26cf5d5be0ac8e8457b8cd7e654a4925329ebb3</originalsourceid><addsrcrecordid>eNo1kUtv1TAQRiMEog_4AWyQl2wS7CROHLFCVUsjtbRCsLb8-HKvL4lzsZ2KiD9PSstqZnE0OpqTZe8YLRhlzcdDcZhCUVLWFlQUlJUvslNGuyangjcv_-00bwVtT7KzGA-UMsZb-jo7KUUneN11p9mfW6i4BEzwicwD0cr81LMH2a82zDv43GJJCG6ZCH6bvfI7EOdJ2oOk9QjS9z2JMAHJzZ7ENSZMxAN2BDmGOWGD78OuJ3olcR6dzWNSCeTr7bc32atBjRFvn-d59uPq8vvFdX5z96W_-HyTo2yqlCtVb7La2mYY7ADbmbritcUwlI0ZuOUaVBkBUfNWC2NbNLxWdVfyquygdXWefXi6u_n8WhCTnFw0GEflMS9Rsq4WLe_aim7o-2d00ROsPAY3qbDK_w_bgE9PADbhB4cgo3HwBtYFmCTt7CSj8jGPPMgtj3zMI6mQW57qL7b4hOo</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1948759730</pqid></control><display><type>article</type><title>Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Chevelkov, Veniamin ; Giller, Karin ; Becker, Stefan ; Lange, Adam</creator><creatorcontrib>Chevelkov, Veniamin ; Giller, Karin ; Becker, Stefan ; Lange, Adam</creatorcontrib><description>[Display omitted]
•We apply the RelaX-EXSY method to measure H/D exchange in a solid state protein.•The method requires proton detection and performs better at higher external magnetic fields.•Amide exchange rates are measured in deuterated Salmonella typhimurium type iii secretion system (T3SS) needles.
In this report we present site-specific measurements of amide hydrogen-deuterium exchange rates in a protein in the solid state phase by MAS NMR. Employing perdeuteration, proton detection and a high external magnetic field we could adopt the highly efficient Relax-EXSY protocol previously developed for liquid state NMR. According to this method, we measured the contribution of hydrogen exchange on apparent 15N longitudinal relaxation rates in samples with differing D2O buffer content. Differences in the apparent T1 times allowed us to derive exchange rates for multiple residues in the type III secretion system needle protein.</description><identifier>ISSN: 1090-7807</identifier><identifier>EISSN: 1096-0856</identifier><identifier>DOI: 10.1016/j.jmr.2017.08.012</identifier><identifier>PMID: 28985499</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amide protons ; Amides - chemistry ; Deuteration ; Deuterium - chemistry ; Deuterium Exchange Measurement - methods ; Deuterium Oxide ; Electromagnetic Fields ; H/D exchange ; Hydrogen - chemistry ; Ion Exchange ; Magic-angle spinning solid-state NMR ; Magnetic Resonance Spectroscopy - methods ; Models, Molecular ; Nitrogen Isotopes ; PrgI ; Proton detection ; Protons ; Relax-EXSY ; Relaxation</subject><ispartof>Journal of magnetic resonance (1997), 2017-10, Vol.283, p.110-116</ispartof><rights>2017 The Authors</rights><rights>Copyright © 2017 The Authors. Published by Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jmr.2017.08.012$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28985499$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chevelkov, Veniamin</creatorcontrib><creatorcontrib>Giller, Karin</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Lange, Adam</creatorcontrib><title>Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR</title><title>Journal of magnetic resonance (1997)</title><addtitle>J Magn Reson</addtitle><description>[Display omitted]
•We apply the RelaX-EXSY method to measure H/D exchange in a solid state protein.•The method requires proton detection and performs better at higher external magnetic fields.•Amide exchange rates are measured in deuterated Salmonella typhimurium type iii secretion system (T3SS) needles.
In this report we present site-specific measurements of amide hydrogen-deuterium exchange rates in a protein in the solid state phase by MAS NMR. Employing perdeuteration, proton detection and a high external magnetic field we could adopt the highly efficient Relax-EXSY protocol previously developed for liquid state NMR. According to this method, we measured the contribution of hydrogen exchange on apparent 15N longitudinal relaxation rates in samples with differing D2O buffer content. Differences in the apparent T1 times allowed us to derive exchange rates for multiple residues in the type III secretion system needle protein.</description><subject>Amide protons</subject><subject>Amides - chemistry</subject><subject>Deuteration</subject><subject>Deuterium - chemistry</subject><subject>Deuterium Exchange Measurement - methods</subject><subject>Deuterium Oxide</subject><subject>Electromagnetic Fields</subject><subject>H/D exchange</subject><subject>Hydrogen - chemistry</subject><subject>Ion Exchange</subject><subject>Magic-angle spinning solid-state NMR</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Models, Molecular</subject><subject>Nitrogen Isotopes</subject><subject>PrgI</subject><subject>Proton detection</subject><subject>Protons</subject><subject>Relax-EXSY</subject><subject>Relaxation</subject><issn>1090-7807</issn><issn>1096-0856</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kUtv1TAQRiMEog_4AWyQl2wS7CROHLFCVUsjtbRCsLb8-HKvL4lzsZ2KiD9PSstqZnE0OpqTZe8YLRhlzcdDcZhCUVLWFlQUlJUvslNGuyangjcv_-00bwVtT7KzGA-UMsZb-jo7KUUneN11p9mfW6i4BEzwicwD0cr81LMH2a82zDv43GJJCG6ZCH6bvfI7EOdJ2oOk9QjS9z2JMAHJzZ7ENSZMxAN2BDmGOWGD78OuJ3olcR6dzWNSCeTr7bc32atBjRFvn-d59uPq8vvFdX5z96W_-HyTo2yqlCtVb7La2mYY7ADbmbritcUwlI0ZuOUaVBkBUfNWC2NbNLxWdVfyquygdXWefXi6u_n8WhCTnFw0GEflMS9Rsq4WLe_aim7o-2d00ROsPAY3qbDK_w_bgE9PADbhB4cgo3HwBtYFmCTt7CSj8jGPPMgtj3zMI6mQW57qL7b4hOo</recordid><startdate>201710</startdate><enddate>201710</enddate><creator>Chevelkov, Veniamin</creator><creator>Giller, Karin</creator><creator>Becker, Stefan</creator><creator>Lange, Adam</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>201710</creationdate><title>Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR</title><author>Chevelkov, Veniamin ; Giller, Karin ; Becker, Stefan ; Lange, Adam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e263t-aa4854bdd6ffdfed9c4354deff26cf5d5be0ac8e8457b8cd7e654a4925329ebb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amide protons</topic><topic>Amides - chemistry</topic><topic>Deuteration</topic><topic>Deuterium - chemistry</topic><topic>Deuterium Exchange Measurement - methods</topic><topic>Deuterium Oxide</topic><topic>Electromagnetic Fields</topic><topic>H/D exchange</topic><topic>Hydrogen - chemistry</topic><topic>Ion Exchange</topic><topic>Magic-angle spinning solid-state NMR</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Models, Molecular</topic><topic>Nitrogen Isotopes</topic><topic>PrgI</topic><topic>Proton detection</topic><topic>Protons</topic><topic>Relax-EXSY</topic><topic>Relaxation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chevelkov, Veniamin</creatorcontrib><creatorcontrib>Giller, Karin</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Lange, Adam</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of magnetic resonance (1997)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chevelkov, Veniamin</au><au>Giller, Karin</au><au>Becker, Stefan</au><au>Lange, Adam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR</atitle><jtitle>Journal of magnetic resonance (1997)</jtitle><addtitle>J Magn Reson</addtitle><date>2017-10</date><risdate>2017</risdate><volume>283</volume><spage>110</spage><epage>116</epage><pages>110-116</pages><issn>1090-7807</issn><eissn>1096-0856</eissn><abstract>[Display omitted]
•We apply the RelaX-EXSY method to measure H/D exchange in a solid state protein.•The method requires proton detection and performs better at higher external magnetic fields.•Amide exchange rates are measured in deuterated Salmonella typhimurium type iii secretion system (T3SS) needles.
In this report we present site-specific measurements of amide hydrogen-deuterium exchange rates in a protein in the solid state phase by MAS NMR. Employing perdeuteration, proton detection and a high external magnetic field we could adopt the highly efficient Relax-EXSY protocol previously developed for liquid state NMR. According to this method, we measured the contribution of hydrogen exchange on apparent 15N longitudinal relaxation rates in samples with differing D2O buffer content. Differences in the apparent T1 times allowed us to derive exchange rates for multiple residues in the type III secretion system needle protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>28985499</pmid><doi>10.1016/j.jmr.2017.08.012</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1090-7807 |
| ispartof | Journal of magnetic resonance (1997), 2017-10, Vol.283, p.110-116 |
| issn | 1090-7807 1096-0856 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1948759730 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amide protons Amides - chemistry Deuteration Deuterium - chemistry Deuterium Exchange Measurement - methods Deuterium Oxide Electromagnetic Fields H/D exchange Hydrogen - chemistry Ion Exchange Magic-angle spinning solid-state NMR Magnetic Resonance Spectroscopy - methods Models, Molecular Nitrogen Isotopes PrgI Proton detection Protons Relax-EXSY Relaxation |
| title | Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T07%3A09%3A08IST&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=Measurement%20of%20backbone%20hydrogen-deuterium%20exchange%20in%20the%20type%20III%20secretion%20system%20needle%20protein%20PrgI%20by%20solid-state%20NMR&rft.jtitle=Journal%20of%20magnetic%20resonance%20(1997)&rft.au=Chevelkov,%20Veniamin&rft.date=2017-10&rft.volume=283&rft.spage=110&rft.epage=116&rft.pages=110-116&rft.issn=1090-7807&rft.eissn=1096-0856&rft_id=info:doi/10.1016/j.jmr.2017.08.012&rft_dat=%3Cproquest_pubme%3E1948759730%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=1948759730&rft_id=info:pmid/28985499&rft_els_id=S1090780717302203&rfr_iscdi=true |