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Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G
Protein dynamics occurring on a wide range of timescales play a crucial role in governing protein function. Particularly, motions between the globular rotational correlation time (τc ) and 40 μs (supra‐τc window), strongly influence molecular recognition. This supra‐τc window was previously hidden,...
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| Published in: | Angewandte Chemie 2016-08, Vol.128 (33), p.9719-9722 |
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| Main Authors: | , , , , , , , |
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| cites | cdi_FETCH-LOGICAL-c3271-f72d3bce4c431b4d6879fd1e3c75bde9df1695d6c8ad5aa5c7ae00b99d821c003 |
| container_end_page | 9722 |
| container_issue | 33 |
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| container_title | Angewandte Chemie |
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| creator | Pratihar, Supriya Sabo, T. Michael Ban, David Fenwick, R. Bryn Becker, Stefan Salvatella, Xavier Griesinger, Christian Lee, Donghan |
| description | Protein dynamics occurring on a wide range of timescales play a crucial role in governing protein function. Particularly, motions between the globular rotational correlation time (τc
) and 40 μs (supra‐τc
window), strongly influence molecular recognition. This supra‐τc
window was previously hidden, owing to a lack of experimental methods. Recently, we have developed a high‐power relaxation dispersion (RD) experiment for measuring kinetics as fast as 4 μs. For the first time, this method, performed under super‐cooled conditions, enabled us to detect a global motion in the first β‐turn of the third IgG‐binding domain of protein G (GB3), which was extrapolated to 371±115 ns at 310 K. Furthermore, the same residues show the plasticity in the model‐free residual dipolar coupling (RDC) order parameters and in an ensemble encoding the supra‐τc
dynamics. This β‐turn is involved in antibody binding, exhibiting the potential link of the observed supra‐τc
motion with molecular recognition.
Übergänge innerhalb des Grundzustandsensembles und molekulare Erkennung hängen zusammen: Mittels Hochleistungsrelaxationsdispersionsexperimenten in stark unterkühltem Wasser kann die Supra‐
‐Dynamik der dritten IgG‐Bindedomäne von Protein G mit deren molekularer Erkennung in Verbindung gebracht werden. |
| doi_str_mv | 10.1002/ange.201603501 |
| format | article |
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) and 40 μs (supra‐τc
window), strongly influence molecular recognition. This supra‐τc
window was previously hidden, owing to a lack of experimental methods. Recently, we have developed a high‐power relaxation dispersion (RD) experiment for measuring kinetics as fast as 4 μs. For the first time, this method, performed under super‐cooled conditions, enabled us to detect a global motion in the first β‐turn of the third IgG‐binding domain of protein G (GB3), which was extrapolated to 371±115 ns at 310 K. Furthermore, the same residues show the plasticity in the model‐free residual dipolar coupling (RDC) order parameters and in an ensemble encoding the supra‐τc
dynamics. This β‐turn is involved in antibody binding, exhibiting the potential link of the observed supra‐τc
motion with molecular recognition.
Übergänge innerhalb des Grundzustandsensembles und molekulare Erkennung hängen zusammen: Mittels Hochleistungsrelaxationsdispersionsexperimenten in stark unterkühltem Wasser kann die Supra‐
‐Dynamik der dritten IgG‐Bindedomäne von Protein G mit deren molekularer Erkennung in Verbindung gebracht werden.</description><identifier>ISSN: 0044-8249</identifier><identifier>EISSN: 1521-3757</identifier><identifier>DOI: 10.1002/ange.201603501</identifier><language>eng ; ger</language><publisher>Weinheim: Blackwell Publishing Ltd</publisher><subject>Antibodies ; Binding ; Chemistry ; Coupling (molecular) ; Dynamics ; Experimental methods ; Extrapolation ; Immunoglobulin G ; Kinetics ; NMR-Spektroskopie ; Order parameters ; Protein G ; Proteindynamik ; Proteins ; Reaktionskinetik ; Recognition ; Relaxationsdispersion ; Residues ; Windows (intervals)</subject><ispartof>Angewandte Chemie, 2016-08, Vol.128 (33), p.9719-9722</ispartof><rights>2016 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3271-f72d3bce4c431b4d6879fd1e3c75bde9df1695d6c8ad5aa5c7ae00b99d821c003</citedby><cites>FETCH-LOGICAL-c3271-f72d3bce4c431b4d6879fd1e3c75bde9df1695d6c8ad5aa5c7ae00b99d821c003</cites><orcidid>0000-0002-1266-4344 ; 0000-0002-9573-145X ; 0000-0002-4993-7983 ; 0000-0002-8371-4185 ; 0000-0002-0925-7422</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%2Fange.201603501$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fange.201603501$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,786,790,27957,27958,50923,51032</link.rule.ids></links><search><creatorcontrib>Pratihar, Supriya</creatorcontrib><creatorcontrib>Sabo, T. Michael</creatorcontrib><creatorcontrib>Ban, David</creatorcontrib><creatorcontrib>Fenwick, R. Bryn</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Salvatella, Xavier</creatorcontrib><creatorcontrib>Griesinger, Christian</creatorcontrib><creatorcontrib>Lee, Donghan</creatorcontrib><title>Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G</title><title>Angewandte Chemie</title><addtitle>Angew. Chem</addtitle><description>Protein dynamics occurring on a wide range of timescales play a crucial role in governing protein function. Particularly, motions between the globular rotational correlation time (τc
) and 40 μs (supra‐τc
window), strongly influence molecular recognition. This supra‐τc
window was previously hidden, owing to a lack of experimental methods. Recently, we have developed a high‐power relaxation dispersion (RD) experiment for measuring kinetics as fast as 4 μs. For the first time, this method, performed under super‐cooled conditions, enabled us to detect a global motion in the first β‐turn of the third IgG‐binding domain of protein G (GB3), which was extrapolated to 371±115 ns at 310 K. Furthermore, the same residues show the plasticity in the model‐free residual dipolar coupling (RDC) order parameters and in an ensemble encoding the supra‐τc
dynamics. This β‐turn is involved in antibody binding, exhibiting the potential link of the observed supra‐τc
motion with molecular recognition.
Übergänge innerhalb des Grundzustandsensembles und molekulare Erkennung hängen zusammen: Mittels Hochleistungsrelaxationsdispersionsexperimenten in stark unterkühltem Wasser kann die Supra‐
‐Dynamik der dritten IgG‐Bindedomäne von Protein G mit deren molekularer Erkennung in Verbindung gebracht werden.</description><subject>Antibodies</subject><subject>Binding</subject><subject>Chemistry</subject><subject>Coupling (molecular)</subject><subject>Dynamics</subject><subject>Experimental methods</subject><subject>Extrapolation</subject><subject>Immunoglobulin G</subject><subject>Kinetics</subject><subject>NMR-Spektroskopie</subject><subject>Order parameters</subject><subject>Protein G</subject><subject>Proteindynamik</subject><subject>Proteins</subject><subject>Reaktionskinetik</subject><subject>Recognition</subject><subject>Relaxationsdispersion</subject><subject>Residues</subject><subject>Windows (intervals)</subject><issn>0044-8249</issn><issn>1521-3757</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhi0EEkvhyjkSFy5ZZuI4jo_bD9Kq1VJBAakXy7EnW5ddu7Wzgv33pCyqEAc4zUjzPK9Gehl7jTBHgOqdCSuaV4ANcAH4hM1QVFhyKeRTNgOo67KtavWcvcj5FgCaSqoZ-3LuA43e5iIOxXhDxSKMvo9uV3wkG1fBjz6G4pMfqfDhF3B145MrzlZdeeiD82FVHMeNmY5TwGWKI01r95I9G8w606vf84B9fn9ydXRaXnzozo4WF6XllcRykJXjvaXa1hz72jWtVIND4laK3pFyAzZKuMa2xgljhJWGAHqlXFuhBeAH7O0-9y7F-y3lUW98trRem0BxmzW2XAgJSvAJffMXehu3KUzfaVSNbBus5b-pFkFwlFBP1HxP2RRzTjTou-Q3Ju00gn4oQz-UoR_LmAS1F777Ne3-Q-vFsjv50y33rs8j_Xh0TfqmGznVq78uO324PL5enl9f6lP-E0pumv0</recordid><startdate>20160808</startdate><enddate>20160808</enddate><creator>Pratihar, Supriya</creator><creator>Sabo, T. Michael</creator><creator>Ban, David</creator><creator>Fenwick, R. Bryn</creator><creator>Becker, Stefan</creator><creator>Salvatella, Xavier</creator><creator>Griesinger, Christian</creator><creator>Lee, Donghan</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><orcidid>https://orcid.org/0000-0002-1266-4344</orcidid><orcidid>https://orcid.org/0000-0002-9573-145X</orcidid><orcidid>https://orcid.org/0000-0002-4993-7983</orcidid><orcidid>https://orcid.org/0000-0002-8371-4185</orcidid><orcidid>https://orcid.org/0000-0002-0925-7422</orcidid></search><sort><creationdate>20160808</creationdate><title>Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G</title><author>Pratihar, Supriya ; Sabo, T. Michael ; Ban, David ; Fenwick, R. Bryn ; Becker, Stefan ; Salvatella, Xavier ; Griesinger, Christian ; Lee, Donghan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3271-f72d3bce4c431b4d6879fd1e3c75bde9df1695d6c8ad5aa5c7ae00b99d821c003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng ; ger</language><creationdate>2016</creationdate><topic>Antibodies</topic><topic>Binding</topic><topic>Chemistry</topic><topic>Coupling (molecular)</topic><topic>Dynamics</topic><topic>Experimental methods</topic><topic>Extrapolation</topic><topic>Immunoglobulin G</topic><topic>Kinetics</topic><topic>NMR-Spektroskopie</topic><topic>Order parameters</topic><topic>Protein G</topic><topic>Proteindynamik</topic><topic>Proteins</topic><topic>Reaktionskinetik</topic><topic>Recognition</topic><topic>Relaxationsdispersion</topic><topic>Residues</topic><topic>Windows (intervals)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pratihar, Supriya</creatorcontrib><creatorcontrib>Sabo, T. Michael</creatorcontrib><creatorcontrib>Ban, David</creatorcontrib><creatorcontrib>Fenwick, R. Bryn</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Salvatella, Xavier</creatorcontrib><creatorcontrib>Griesinger, Christian</creatorcontrib><creatorcontrib>Lee, Donghan</creatorcontrib><collection>Istex</collection><collection>CrossRef</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>Angewandte Chemie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pratihar, Supriya</au><au>Sabo, T. Michael</au><au>Ban, David</au><au>Fenwick, R. Bryn</au><au>Becker, Stefan</au><au>Salvatella, Xavier</au><au>Griesinger, Christian</au><au>Lee, Donghan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G</atitle><jtitle>Angewandte Chemie</jtitle><addtitle>Angew. Chem</addtitle><date>2016-08-08</date><risdate>2016</risdate><volume>128</volume><issue>33</issue><spage>9719</spage><epage>9722</epage><pages>9719-9722</pages><issn>0044-8249</issn><eissn>1521-3757</eissn><notes>EU</notes><notes>MINECO - No. BIO2012-31043</notes><notes>James Graham Brown Foundation</notes><notes>Max Planck Society</notes><notes>ArticleID:ANGE201603501</notes><notes>ERC - No. 233227</notes><notes>istex:D722924D5E3F59CE936FE33C1A178898E4D4250D</notes><notes>ark:/67375/WNG-BNDZNKZP-H</notes><notes>These authors contributed equally to this work.</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Protein dynamics occurring on a wide range of timescales play a crucial role in governing protein function. Particularly, motions between the globular rotational correlation time (τc
) and 40 μs (supra‐τc
window), strongly influence molecular recognition. This supra‐τc
window was previously hidden, owing to a lack of experimental methods. Recently, we have developed a high‐power relaxation dispersion (RD) experiment for measuring kinetics as fast as 4 μs. For the first time, this method, performed under super‐cooled conditions, enabled us to detect a global motion in the first β‐turn of the third IgG‐binding domain of protein G (GB3), which was extrapolated to 371±115 ns at 310 K. Furthermore, the same residues show the plasticity in the model‐free residual dipolar coupling (RDC) order parameters and in an ensemble encoding the supra‐τc
dynamics. This β‐turn is involved in antibody binding, exhibiting the potential link of the observed supra‐τc
motion with molecular recognition.
Übergänge innerhalb des Grundzustandsensembles und molekulare Erkennung hängen zusammen: Mittels Hochleistungsrelaxationsdispersionsexperimenten in stark unterkühltem Wasser kann die Supra‐
‐Dynamik der dritten IgG‐Bindedomäne von Protein G mit deren molekularer Erkennung in Verbindung gebracht werden.</abstract><cop>Weinheim</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1002/ange.201603501</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-1266-4344</orcidid><orcidid>https://orcid.org/0000-0002-9573-145X</orcidid><orcidid>https://orcid.org/0000-0002-4993-7983</orcidid><orcidid>https://orcid.org/0000-0002-8371-4185</orcidid><orcidid>https://orcid.org/0000-0002-0925-7422</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0044-8249 |
| ispartof | Angewandte Chemie, 2016-08, Vol.128 (33), p.9719-9722 |
| issn | 0044-8249 1521-3757 |
| language | eng ; ger |
| recordid | cdi_proquest_miscellaneous_1835570953 |
| source | Wiley-Blackwell Journals |
| subjects | Antibodies Binding Chemistry Coupling (molecular) Dynamics Experimental methods Extrapolation Immunoglobulin G Kinetics NMR-Spektroskopie Order parameters Protein G Proteindynamik Proteins Reaktionskinetik Recognition Relaxationsdispersion Residues Windows (intervals) |
| title | Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G |
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