1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis
We report the nearly complete 1 H, 13 C, and 15 N resonance assignments of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitides . Secondary structure determination using CSI method leads to the prediction of nine β-sheet parts.
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| Veröffentlicht in: | Biomolecular NMR assignments 2008-06, Vol.2 (1), p.85-87 |
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| container_issue | 1 |
| container_start_page | 85 |
| container_title | Biomolecular NMR assignments |
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| creator | Quinternet, Marc Selme, Laure Beaufils, Chrystel Tsan, Pascale Jacob, Christophe Boschi-Muller, Sandrine Averlant-Petit, Marie-Christine Branlant, Guy Cung, Manh-Thong |
| description | We report the nearly complete
1
H,
13
C, and
15
N resonance assignments of the C103S mutant of the N-terminal domain of DsbD from
Neisseria meningitides
. Secondary structure determination using CSI method leads to the prediction of nine β-sheet parts. |
| doi_str_mv | 10.1007/s12104-008-9091-y |
| format | Article |
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1
H,
13
C, and
15
N resonance assignments of the C103S mutant of the N-terminal domain of DsbD from
Neisseria meningitides
. Secondary structure determination using CSI method leads to the prediction of nine β-sheet parts.</description><identifier>ISSN: 1874-2718</identifier><identifier>EISSN: 1874-270X</identifier><identifier>DOI: 10.1007/s12104-008-9091-y</identifier><identifier>PMID: 19636931</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Amino Acid Sequence ; Antigens, Bacterial ; Antigens, Bacterial - chemistry ; Bacteria ; Bacterial Proteins ; Bacterial Proteins - chemistry ; Biochemistry ; Biochemistry, Molecular Biology ; Biological and Medical Physics ; Biophysics ; Carbon Isotopes ; Carbon Isotopes - chemistry ; E coli ; Life Sciences ; Magnetic Resonance Spectroscopy ; Magnetic Resonance Spectroscopy - methods ; Molecular biology ; Molecular Sequence Data ; Molecular Weight ; Mutagenesis, Site-Directed ; Mutation ; Neisseria meningitidis ; Neisseria meningitidis - genetics ; Neisseria meningitidis - metabolism ; Nitrogen Isotopes ; Nitrogen Isotopes - chemistry ; NMR ; Nuclear magnetic resonance ; Physics ; Physics and Astronomy ; Polymer Sciences ; Proteins ; Protons ; Structural Biology</subject><ispartof>Biomolecular NMR assignments, 2008-06, Vol.2 (1), p.85-87</ispartof><rights>Springer Science+Business Media B.V. 2008</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c248y-497b565fa2cbfff9c9ee1293d89d62fbffe441f2b879ffafeb1deb6c03e99af13</citedby><cites>FETCH-LOGICAL-c248y-497b565fa2cbfff9c9ee1293d89d62fbffe441f2b879ffafeb1deb6c03e99af13</cites><orcidid>0000-0001-8956-1231 ; 0000-0002-8299-7136 ; 0000-0001-8522-2865 ; 0000-0001-8962-4749</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12104-008-9091-y$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12104-008-9091-y$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27903,27904,41467,42536,51298</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19636931$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00433190$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Quinternet, Marc</creatorcontrib><creatorcontrib>Selme, Laure</creatorcontrib><creatorcontrib>Beaufils, Chrystel</creatorcontrib><creatorcontrib>Tsan, Pascale</creatorcontrib><creatorcontrib>Jacob, Christophe</creatorcontrib><creatorcontrib>Boschi-Muller, Sandrine</creatorcontrib><creatorcontrib>Averlant-Petit, Marie-Christine</creatorcontrib><creatorcontrib>Branlant, Guy</creatorcontrib><creatorcontrib>Cung, Manh-Thong</creatorcontrib><title>1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis</title><title>Biomolecular NMR assignments</title><addtitle>Biomol NMR Assign</addtitle><addtitle>Biomol NMR Assign</addtitle><description>We report the nearly complete
1
H,
13
C, and
15
N resonance assignments of the C103S mutant of the N-terminal domain of DsbD from
Neisseria meningitides
. Secondary structure determination using CSI method leads to the prediction of nine β-sheet parts.</description><subject>Amino Acid Sequence</subject><subject>Antigens, Bacterial</subject><subject>Antigens, Bacterial - chemistry</subject><subject>Bacteria</subject><subject>Bacterial Proteins</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Carbon Isotopes</subject><subject>Carbon Isotopes - chemistry</subject><subject>E coli</subject><subject>Life Sciences</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Neisseria meningitidis</subject><subject>Neisseria meningitidis - genetics</subject><subject>Neisseria meningitidis - metabolism</subject><subject>Nitrogen Isotopes</subject><subject>Nitrogen Isotopes - chemistry</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Polymer Sciences</subject><subject>Proteins</subject><subject>Protons</subject><subject>Structural Biology</subject><issn>1874-2718</issn><issn>1874-270X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kcFO3DAQhi1EVSj0AbggixsSKTN2NomPaGm7lVbLASr1ZjnJeDHaOGBnkfbtcZQVe-rJ1sw338j-GbtA-IEA5W1EgZBnAFWmQGG2O2KnWJV5Jkr4d_x5x-qEfYvxBaAQIPArO0FVyEJJPGXvuLjhKOc33PiW42zFA8XeG98QNzG6te_ID7y3fHgmPkeQj7zbDuZQW2UDhc55s-Ft3xnnx8Z9rO-5DX3HV-RipOAMTyLn125wrYvn7Is1m0jf9-cZ-_vr59N8kS0ffv-Z3y2zRuTVLstVWc-KmTWiqa21qlFEKJRsK9UWwqYa5TlaUVelstZYqrGlumhAklLGojxj15P32Wz0a3CdCTvdG6cXd0s91gByKVHB-8heTexr6N-2FAf90m9DelfUAjB9-ExUCcIJakIfYyD7aUXQYyh6CiWJKz2Gondp5nIv3tYdtYeJfQoJEBMQU8uvKRw2_9_6AXFvlnQ</recordid><startdate>200806</startdate><enddate>200806</enddate><creator>Quinternet, Marc</creator><creator>Selme, Laure</creator><creator>Beaufils, Chrystel</creator><creator>Tsan, Pascale</creator><creator>Jacob, Christophe</creator><creator>Boschi-Muller, Sandrine</creator><creator>Averlant-Petit, Marie-Christine</creator><creator>Branlant, Guy</creator><creator>Cung, Manh-Thong</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><general>Springer</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>K9.</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0001-8956-1231</orcidid><orcidid>https://orcid.org/0000-0002-8299-7136</orcidid><orcidid>https://orcid.org/0000-0001-8522-2865</orcidid><orcidid>https://orcid.org/0000-0001-8962-4749</orcidid></search><sort><creationdate>200806</creationdate><title>1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis</title><author>Quinternet, Marc ; Selme, Laure ; Beaufils, Chrystel ; Tsan, Pascale ; Jacob, Christophe ; Boschi-Muller, Sandrine ; Averlant-Petit, Marie-Christine ; Branlant, Guy ; Cung, Manh-Thong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c248y-497b565fa2cbfff9c9ee1293d89d62fbffe441f2b879ffafeb1deb6c03e99af13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Antigens, Bacterial</topic><topic>Antigens, Bacterial - chemistry</topic><topic>Bacteria</topic><topic>Bacterial Proteins</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Carbon Isotopes</topic><topic>Carbon Isotopes - chemistry</topic><topic>E coli</topic><topic>Life Sciences</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Molecular biology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Neisseria meningitidis</topic><topic>Neisseria meningitidis - genetics</topic><topic>Neisseria meningitidis - metabolism</topic><topic>Nitrogen Isotopes</topic><topic>Nitrogen Isotopes - chemistry</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Polymer Sciences</topic><topic>Proteins</topic><topic>Protons</topic><topic>Structural Biology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quinternet, Marc</creatorcontrib><creatorcontrib>Selme, Laure</creatorcontrib><creatorcontrib>Beaufils, Chrystel</creatorcontrib><creatorcontrib>Tsan, Pascale</creatorcontrib><creatorcontrib>Jacob, Christophe</creatorcontrib><creatorcontrib>Boschi-Muller, Sandrine</creatorcontrib><creatorcontrib>Averlant-Petit, Marie-Christine</creatorcontrib><creatorcontrib>Branlant, Guy</creatorcontrib><creatorcontrib>Cung, Manh-Thong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Biomolecular NMR assignments</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Quinternet, Marc</au><au>Selme, Laure</au><au>Beaufils, Chrystel</au><au>Tsan, Pascale</au><au>Jacob, Christophe</au><au>Boschi-Muller, Sandrine</au><au>Averlant-Petit, Marie-Christine</au><au>Branlant, Guy</au><au>Cung, Manh-Thong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis</atitle><jtitle>Biomolecular NMR assignments</jtitle><stitle>Biomol NMR Assign</stitle><addtitle>Biomol NMR Assign</addtitle><date>2008-06</date><risdate>2008</risdate><volume>2</volume><issue>1</issue><spage>85</spage><epage>87</epage><pages>85-87</pages><issn>1874-2718</issn><eissn>1874-270X</eissn><abstract>We report the nearly complete
1
H,
13
C, and
15
N resonance assignments of the C103S mutant of the N-terminal domain of DsbD from
Neisseria meningitides
. Secondary structure determination using CSI method leads to the prediction of nine β-sheet parts.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>19636931</pmid><doi>10.1007/s12104-008-9091-y</doi><tpages>3</tpages><orcidid>https://orcid.org/0000-0001-8956-1231</orcidid><orcidid>https://orcid.org/0000-0002-8299-7136</orcidid><orcidid>https://orcid.org/0000-0001-8522-2865</orcidid><orcidid>https://orcid.org/0000-0001-8962-4749</orcidid></addata></record> |
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| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_00433190v1 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Amino Acid Sequence Antigens, Bacterial Antigens, Bacterial - chemistry Bacteria Bacterial Proteins Bacterial Proteins - chemistry Biochemistry Biochemistry, Molecular Biology Biological and Medical Physics Biophysics Carbon Isotopes Carbon Isotopes - chemistry E coli Life Sciences Magnetic Resonance Spectroscopy Magnetic Resonance Spectroscopy - methods Molecular biology Molecular Sequence Data Molecular Weight Mutagenesis, Site-Directed Mutation Neisseria meningitidis Neisseria meningitidis - genetics Neisseria meningitidis - metabolism Nitrogen Isotopes Nitrogen Isotopes - chemistry NMR Nuclear magnetic resonance Physics Physics and Astronomy Polymer Sciences Proteins Protons Structural Biology |
| title | 1H, 13C, and 15N resonance assignment of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis |
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