High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy
High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by...
Gespeichert in:
| Veröffentlicht in: | PloS one 2008-06, Vol.3 (6), p.e2359-e2359 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e2359 |
|---|---|
| container_issue | 6 |
| container_start_page | e2359 |
| container_title | PloS one |
| container_volume | 3 |
| creator | Korukottu, Jegannath Schneider, Robert Vijayan, Vinesh Lange, Adam Pongs, Olaf Becker, Stefan Baldus, Marc Zweckstetter, Markus |
| description | High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins. |
| doi_str_mv | 10.1371/journal.pone.0002359 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1312288885</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A472648902</galeid><doaj_id>oai_doaj_org_article_a40d50c72cbb4cc3b5fbac40719df181</doaj_id><sourcerecordid>A472648902</sourcerecordid><originalsourceid>FETCH-LOGICAL-c662t-414935e7d21916375b7a9a6c769ce4a4868f9be6789ffd9362131ad5f9ef2dce3</originalsourceid><addsrcrecordid>eNqNkttu1DAQhiMEoqXwBggiIVXiIosPiR3fIFXl0JUKlcpB3FmOM971ko2D7aDu2-PtprCLuMC-sDX-5h_P6M-ypxjNMOX41cqNvlfdbHA9zBBChFbiXnaMBSUFI4je37sfZY9CWCFU0Zqxh9kRrquE1-w4-3ZhF8vCQ3DdGK3rc_omD9GPOo4e8hYi-LXt1e2TM_l31VkX3Y3t82aTpyTbFiGqCPnHD9d5GEBH74J2w-Zx9sCoLsCT6TzJvrx7-_n8ori8ej8_P7ssNGMkFiUuBa2AtwQLzCivGq6EYpozoaFUZc1qIxpgvBbGtIIygilWbWUEGNJqoCfZ853u0Lkgp6EEmShC6rSqRMx3ROvUSg7erpXfSKesvA04v5DKR6s7kKpEbYU0J7ppSq1pU5lG6RJxLFqDa5y0Xk_VxmYNqX4fveoORA9feruUC_dTElpzxEkSOJ0EvPsxQohybYOGrlM9uDFInoZQ4Zon8MVf4L97m-2ohUrft71xqapOu4W11ckZxqb4WckJK2uBtvVfHiQkJsJNXKgxBDn_dP3_7NXXQ_Z0j12C6uLyzlPhECx3oE5GCR7M7-FhJLfGvutTbo0tJ2OntGf7g_-TNDmZ_gJmx_Uf</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1312288885</pqid></control><display><type>article</type><title>High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy</title><source>MEDLINE</source><source>Public Library of Science (PLoS) Journals Open Access</source><source>DOAJ Directory of Open Access Journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><source>EZB Electronic Journals Library</source><creator>Korukottu, Jegannath ; Schneider, Robert ; Vijayan, Vinesh ; Lange, Adam ; Pongs, Olaf ; Becker, Stefan ; Baldus, Marc ; Zweckstetter, Markus</creator><contributor>Lu, Jianren</contributor><creatorcontrib>Korukottu, Jegannath ; Schneider, Robert ; Vijayan, Vinesh ; Lange, Adam ; Pongs, Olaf ; Becker, Stefan ; Baldus, Marc ; Zweckstetter, Markus ; Lu, Jianren</creatorcontrib><description>High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0002359</identifier><identifier>PMID: 18523586</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amyloid ; Atomic structure ; Biology ; Biophysics ; Biophysics/Experimental Biophysical Methods ; Biophysics/Membrane Proteins and Energy Transduction ; Biophysics/Structural Genomics ; Chemistry ; Crystallography ; Experiments ; High resolution ; Magnetic resonance spectroscopy ; Mathematical analysis ; Membrane proteins ; Models, Molecular ; Molecular Structure ; NMR spectroscopy ; Nuclear magnetic resonance spectroscopy ; Potassium ; Protein structure ; Proteins ; Scorpion Venoms - chemistry ; Solid state ; Spectroscopy ; X-ray crystallography</subject><ispartof>PloS one, 2008-06, Vol.3 (6), p.e2359-e2359</ispartof><rights>COPYRIGHT 2008 Public Library of Science</rights><rights>2008 Korukottu et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Korukottu et al. 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c662t-414935e7d21916375b7a9a6c769ce4a4868f9be6789ffd9362131ad5f9ef2dce3</citedby><cites>FETCH-LOGICAL-c662t-414935e7d21916375b7a9a6c769ce4a4868f9be6789ffd9362131ad5f9ef2dce3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2387072/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2387072/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2929,23868,27926,27927,53793,53795</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18523586$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Lu, Jianren</contributor><creatorcontrib>Korukottu, Jegannath</creatorcontrib><creatorcontrib>Schneider, Robert</creatorcontrib><creatorcontrib>Vijayan, Vinesh</creatorcontrib><creatorcontrib>Lange, Adam</creatorcontrib><creatorcontrib>Pongs, Olaf</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Baldus, Marc</creatorcontrib><creatorcontrib>Zweckstetter, Markus</creatorcontrib><title>High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.</description><subject>Amyloid</subject><subject>Atomic structure</subject><subject>Biology</subject><subject>Biophysics</subject><subject>Biophysics/Experimental Biophysical Methods</subject><subject>Biophysics/Membrane Proteins and Energy Transduction</subject><subject>Biophysics/Structural Genomics</subject><subject>Chemistry</subject><subject>Crystallography</subject><subject>Experiments</subject><subject>High resolution</subject><subject>Magnetic resonance spectroscopy</subject><subject>Mathematical analysis</subject><subject>Membrane proteins</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>NMR spectroscopy</subject><subject>Nuclear magnetic resonance spectroscopy</subject><subject>Potassium</subject><subject>Protein structure</subject><subject>Proteins</subject><subject>Scorpion Venoms - chemistry</subject><subject>Solid state</subject><subject>Spectroscopy</subject><subject>X-ray crystallography</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNkttu1DAQhiMEoqXwBggiIVXiIosPiR3fIFXl0JUKlcpB3FmOM971ko2D7aDu2-PtprCLuMC-sDX-5h_P6M-ypxjNMOX41cqNvlfdbHA9zBBChFbiXnaMBSUFI4je37sfZY9CWCFU0Zqxh9kRrquE1-w4-3ZhF8vCQ3DdGK3rc_omD9GPOo4e8hYi-LXt1e2TM_l31VkX3Y3t82aTpyTbFiGqCPnHD9d5GEBH74J2w-Zx9sCoLsCT6TzJvrx7-_n8ori8ej8_P7ssNGMkFiUuBa2AtwQLzCivGq6EYpozoaFUZc1qIxpgvBbGtIIygilWbWUEGNJqoCfZ853u0Lkgp6EEmShC6rSqRMx3ROvUSg7erpXfSKesvA04v5DKR6s7kKpEbYU0J7ppSq1pU5lG6RJxLFqDa5y0Xk_VxmYNqX4fveoORA9feruUC_dTElpzxEkSOJ0EvPsxQohybYOGrlM9uDFInoZQ4Zon8MVf4L97m-2ohUrft71xqapOu4W11ckZxqb4WckJK2uBtvVfHiQkJsJNXKgxBDn_dP3_7NXXQ_Z0j12C6uLyzlPhECx3oE5GCR7M7-FhJLfGvutTbo0tJ2OntGf7g_-TNDmZ_gJmx_Uf</recordid><startdate>20080604</startdate><enddate>20080604</enddate><creator>Korukottu, Jegannath</creator><creator>Schneider, Robert</creator><creator>Vijayan, Vinesh</creator><creator>Lange, Adam</creator><creator>Pongs, Olaf</creator><creator>Becker, Stefan</creator><creator>Baldus, Marc</creator><creator>Zweckstetter, Markus</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20080604</creationdate><title>High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy</title><author>Korukottu, Jegannath ; Schneider, Robert ; Vijayan, Vinesh ; Lange, Adam ; Pongs, Olaf ; Becker, Stefan ; Baldus, Marc ; Zweckstetter, Markus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c662t-414935e7d21916375b7a9a6c769ce4a4868f9be6789ffd9362131ad5f9ef2dce3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amyloid</topic><topic>Atomic structure</topic><topic>Biology</topic><topic>Biophysics</topic><topic>Biophysics/Experimental Biophysical Methods</topic><topic>Biophysics/Membrane Proteins and Energy Transduction</topic><topic>Biophysics/Structural Genomics</topic><topic>Chemistry</topic><topic>Crystallography</topic><topic>Experiments</topic><topic>High resolution</topic><topic>Magnetic resonance spectroscopy</topic><topic>Mathematical analysis</topic><topic>Membrane proteins</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>NMR spectroscopy</topic><topic>Nuclear magnetic resonance spectroscopy</topic><topic>Potassium</topic><topic>Protein structure</topic><topic>Proteins</topic><topic>Scorpion Venoms - chemistry</topic><topic>Solid state</topic><topic>Spectroscopy</topic><topic>X-ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Korukottu, Jegannath</creatorcontrib><creatorcontrib>Schneider, Robert</creatorcontrib><creatorcontrib>Vijayan, Vinesh</creatorcontrib><creatorcontrib>Lange, Adam</creatorcontrib><creatorcontrib>Pongs, Olaf</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Baldus, Marc</creatorcontrib><creatorcontrib>Zweckstetter, Markus</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Opposing Viewpoints Resource Center</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Proquest Nursing & Allied Health Source</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>https://resources.nclive.org/materials</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>ProQuest Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest advanced technologies & aerospace journals</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials science collection</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Korukottu, Jegannath</au><au>Schneider, Robert</au><au>Vijayan, Vinesh</au><au>Lange, Adam</au><au>Pongs, Olaf</au><au>Becker, Stefan</au><au>Baldus, Marc</au><au>Zweckstetter, Markus</au><au>Lu, Jianren</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2008-06-04</date><risdate>2008</risdate><volume>3</volume><issue>6</issue><spage>e2359</spage><epage>e2359</epage><pages>e2359-e2359</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>High-resolution solid-state NMR spectroscopy can provide structural information of proteins that cannot be studied by X-ray crystallography or solution NMR spectroscopy. Here we demonstrate that it is possible to determine a protein structure by solid-state NMR to a resolution comparable to that by solution NMR. Using an iterative assignment and structure calculation protocol, a large number of distance restraints was extracted from (1)H/(1)H mixing experiments recorded on a single uniformly labeled sample under magic angle spinning conditions. The calculated structure has a coordinate precision of 0.6 A and 1.3 A for the backbone and side chain heavy atoms, respectively, and deviates from the structure observed in solution. The approach is expected to be applicable to larger systems enabling the determination of high-resolution structures of amyloid or membrane proteins.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>18523586</pmid><doi>10.1371/journal.pone.0002359</doi><tpages>e2359</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2008-06, Vol.3 (6), p.e2359-e2359 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1312288885 |
| source | MEDLINE; Public Library of Science (PLoS) Journals Open Access; DOAJ Directory of Open Access Journals; PubMed Central; Free Full-Text Journals in Chemistry; EZB Electronic Journals Library |
| subjects | Amyloid Atomic structure Biology Biophysics Biophysics/Experimental Biophysical Methods Biophysics/Membrane Proteins and Energy Transduction Biophysics/Structural Genomics Chemistry Crystallography Experiments High resolution Magnetic resonance spectroscopy Mathematical analysis Membrane proteins Models, Molecular Molecular Structure NMR spectroscopy Nuclear magnetic resonance spectroscopy Potassium Protein structure Proteins Scorpion Venoms - chemistry Solid state Spectroscopy X-ray crystallography |
| title | High-resolution 3D structure determination of kaliotoxin by solid-state NMR spectroscopy |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-17T19%3A25%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=High-resolution%203D%20structure%20determination%20of%20kaliotoxin%20by%20solid-state%20NMR%20spectroscopy&rft.jtitle=PloS%20one&rft.au=Korukottu,%20Jegannath&rft.date=2008-06-04&rft.volume=3&rft.issue=6&rft.spage=e2359&rft.epage=e2359&rft.pages=e2359-e2359&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0002359&rft_dat=%3Cgale_plos_%3EA472648902%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1312288885&rft_id=info:pmid/18523586&rft_galeid=A472648902&rft_doaj_id=oai_doaj_org_article_a40d50c72cbb4cc3b5fbac40719df181&rfr_iscdi=true |