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Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter
Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate C and N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly...
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Published in: | Chemphyschem 2020-07, Vol.21 (13), p.1436-1443 |
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creator | Kraus, Jodi Gupta, Rupal Lu, Manman Gronenborn, Angela M Akke, Mikael Polenova, Tatyana |
description | Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate
C and
N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for
N atoms. Here we compare experimentally determined backbone
C
and
N
chemical shift tensors by MAS NMR with hybrid quantum mechanics/molecular mechanics/molecular dynamics (MD-QM/MM) calculations for the carbohydrate-binding domain of galectin-3. Excellent agreement between experimental and computed
N
chemical shift anisotropy values was obtained using the Amber ff15ipq force field when solvent dynamics was taken into account in the calculation. Our results establish important benchmark conditions for improving the accuracy of chemical shift calculations in proteins and may aid in the validation of protein structure models derived by MAS NMR. |
doi_str_mv | 10.1002/cphc.202000249 |
format | article |
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C and
N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for
N atoms. Here we compare experimentally determined backbone
C
and
N
chemical shift tensors by MAS NMR with hybrid quantum mechanics/molecular mechanics/molecular dynamics (MD-QM/MM) calculations for the carbohydrate-binding domain of galectin-3. Excellent agreement between experimental and computed
N
chemical shift anisotropy values was obtained using the Amber ff15ipq force field when solvent dynamics was taken into account in the calculation. Our results establish important benchmark conditions for improving the accuracy of chemical shift calculations in proteins and may aid in the validation of protein structure models derived by MAS NMR.</description><identifier>ISSN: 1439-4235</identifier><identifier>EISSN: 1439-7641</identifier><identifier>DOI: 10.1002/cphc.202000249</identifier><identifier>PMID: 32363727</identifier><language>eng</language><publisher>Germany</publisher><subject>Blood Proteins - chemistry ; Carbon Isotopes - chemistry ; Density Functional Theory ; Galectins - chemistry ; Humans ; Models, Chemical ; Molecular Dynamics Simulation ; Nitrogen Isotopes - chemistry ; Nuclear Magnetic Resonance, Biomolecular</subject><ispartof>Chemphyschem, 2020-07, Vol.21 (13), p.1436-1443</ispartof><rights>2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1407-72a499dc4709e774785b3085213127542dbce12a164daa48bfa9240e30ef00c23</citedby><cites>FETCH-LOGICAL-c1407-72a499dc4709e774785b3085213127542dbce12a164daa48bfa9240e30ef00c23</cites><orcidid>0000-0001-8637-6129 ; 0000-0002-2395-825X ; 0000-0002-6395-6283 ; 0000-0002-4156-4975 ; 0000-0002-0346-1131 ; 0000-0001-9072-3525</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32363727$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kraus, Jodi</creatorcontrib><creatorcontrib>Gupta, Rupal</creatorcontrib><creatorcontrib>Lu, Manman</creatorcontrib><creatorcontrib>Gronenborn, Angela M</creatorcontrib><creatorcontrib>Akke, Mikael</creatorcontrib><creatorcontrib>Polenova, Tatyana</creatorcontrib><title>Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter</title><title>Chemphyschem</title><addtitle>Chemphyschem</addtitle><description>Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate
C and
N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for
N atoms. Here we compare experimentally determined backbone
C
and
N
chemical shift tensors by MAS NMR with hybrid quantum mechanics/molecular mechanics/molecular dynamics (MD-QM/MM) calculations for the carbohydrate-binding domain of galectin-3. Excellent agreement between experimental and computed
N
chemical shift anisotropy values was obtained using the Amber ff15ipq force field when solvent dynamics was taken into account in the calculation. Our results establish important benchmark conditions for improving the accuracy of chemical shift calculations in proteins and may aid in the validation of protein structure models derived by MAS NMR.</description><subject>Blood Proteins - chemistry</subject><subject>Carbon Isotopes - chemistry</subject><subject>Density Functional Theory</subject><subject>Galectins - chemistry</subject><subject>Humans</subject><subject>Models, Chemical</subject><subject>Molecular Dynamics Simulation</subject><subject>Nitrogen Isotopes - chemistry</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><issn>1439-4235</issn><issn>1439-7641</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNo9kctu2zAQRYmiQe08tl0Ws-xGDl8ype5cNy_ASpDYWQsUNYLZSpRDUgXyGfnjyImT1cxgzpzFXEK-MzpjlPJzs9uaGaecjoPMv5ApkyJP1Fyyr4decpFOyHEIf0cmo4p9IxPBxVworqbkZWHM4HVE-K3Nv6p3CEzAErSrgaVwC8stdtboFtZb20TYoAu9D2AdXOkWTbQuEfAHI_rOOqyheoZisYbb4uHNcV-cF8WvPaBtG6BvYB39YOLg8W1_4f5b37sOXYRCx1FzSo4a3QY8O9QT8nh5sVleJ6u7q5vlYpUYJqlKFNcyz2sjFc1RKamytBI0SzkTjKtU8royyLhmc1lrLbOq0TmXFAXFhlLDxQn5-e7d-f5pwBDLzgaDbasd9kMoucgzNqepkiM6e0eN70Pw2JQ7bzvtn0tGy30M5T6G8jOG8eDHwT1UHdaf-MffxSsGPoAK</recordid><startdate>20200702</startdate><enddate>20200702</enddate><creator>Kraus, Jodi</creator><creator>Gupta, Rupal</creator><creator>Lu, Manman</creator><creator>Gronenborn, Angela M</creator><creator>Akke, Mikael</creator><creator>Polenova, Tatyana</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><orcidid>https://orcid.org/0000-0001-8637-6129</orcidid><orcidid>https://orcid.org/0000-0002-2395-825X</orcidid><orcidid>https://orcid.org/0000-0002-6395-6283</orcidid><orcidid>https://orcid.org/0000-0002-4156-4975</orcidid><orcidid>https://orcid.org/0000-0002-0346-1131</orcidid><orcidid>https://orcid.org/0000-0001-9072-3525</orcidid></search><sort><creationdate>20200702</creationdate><title>Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter</title><author>Kraus, Jodi ; Gupta, Rupal ; Lu, Manman ; Gronenborn, Angela M ; Akke, Mikael ; Polenova, Tatyana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1407-72a499dc4709e774785b3085213127542dbce12a164daa48bfa9240e30ef00c23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Blood Proteins - chemistry</topic><topic>Carbon Isotopes - chemistry</topic><topic>Density Functional Theory</topic><topic>Galectins - chemistry</topic><topic>Humans</topic><topic>Models, Chemical</topic><topic>Molecular Dynamics Simulation</topic><topic>Nitrogen Isotopes - chemistry</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kraus, Jodi</creatorcontrib><creatorcontrib>Gupta, Rupal</creatorcontrib><creatorcontrib>Lu, Manman</creatorcontrib><creatorcontrib>Gronenborn, Angela M</creatorcontrib><creatorcontrib>Akke, Mikael</creatorcontrib><creatorcontrib>Polenova, Tatyana</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>Chemphyschem</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kraus, Jodi</au><au>Gupta, Rupal</au><au>Lu, Manman</au><au>Gronenborn, Angela M</au><au>Akke, Mikael</au><au>Polenova, Tatyana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter</atitle><jtitle>Chemphyschem</jtitle><addtitle>Chemphyschem</addtitle><date>2020-07-02</date><risdate>2020</risdate><volume>21</volume><issue>13</issue><spage>1436</spage><epage>1443</epage><pages>1436-1443</pages><issn>1439-4235</issn><eissn>1439-7641</eissn><abstract>Chemical shift tensors obtained from solid-state NMR spectroscopy are very sensitive reporters of structure and dynamics in proteins. While accurate
C and
N chemical shift tensors are accessible by magic angle spinning (MAS) NMR, their quantum mechanical calculations remain challenging, particularly for
N atoms. Here we compare experimentally determined backbone
C
and
N
chemical shift tensors by MAS NMR with hybrid quantum mechanics/molecular mechanics/molecular dynamics (MD-QM/MM) calculations for the carbohydrate-binding domain of galectin-3. Excellent agreement between experimental and computed
N
chemical shift anisotropy values was obtained using the Amber ff15ipq force field when solvent dynamics was taken into account in the calculation. Our results establish important benchmark conditions for improving the accuracy of chemical shift calculations in proteins and may aid in the validation of protein structure models derived by MAS NMR.</abstract><cop>Germany</cop><pmid>32363727</pmid><doi>10.1002/cphc.202000249</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0001-8637-6129</orcidid><orcidid>https://orcid.org/0000-0002-2395-825X</orcidid><orcidid>https://orcid.org/0000-0002-6395-6283</orcidid><orcidid>https://orcid.org/0000-0002-4156-4975</orcidid><orcidid>https://orcid.org/0000-0002-0346-1131</orcidid><orcidid>https://orcid.org/0000-0001-9072-3525</orcidid></addata></record> |
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subjects | Blood Proteins - chemistry Carbon Isotopes - chemistry Density Functional Theory Galectins - chemistry Humans Models, Chemical Molecular Dynamics Simulation Nitrogen Isotopes - chemistry Nuclear Magnetic Resonance, Biomolecular |
title | Accurate Backbone 13 C and 15 N Chemical Shift Tensors in Galectin-3 Determined by MAS NMR and QM/MM: Details of Structure and Environment Matter |
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