Magic Angle Spinning Solid-State NMR Spectroscopy for Structural Studies of Protein Interfaces. Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation
De novo site-specific backbone and side-chain resonance assignments are presented for U-15N(1-73)/U-13C,15N(74-108) reassembly of Escherichia coli thioredoxin by fragment complementation, determined using solid-state magic angle spinning NMR spectroscopy at 17.6 T. Backbone dihedral angles and secon...
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| Veröffentlicht in: | Journal of the American Chemical Society 2004-12, Vol.126 (50), p.16608-16620 |
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| container_title | Journal of the American Chemical Society |
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| creator | MARULANDA, Dabeiba TASAYCO, Maria Luisa MCDERMOTT, Ann CATALDI, Marcela ARRIARAN, Vilma POLENOVA, Tatyana |
| description | De novo site-specific backbone and side-chain resonance assignments are presented for U-15N(1-73)/U-13C,15N(74-108) reassembly of Escherichia coli thioredoxin by fragment complementation, determined using solid-state magic angle spinning NMR spectroscopy at 17.6 T. Backbone dihedral angles and secondary structure predicted from the statistical analysis of 13C and 15N chemical shifts are in general agreement with solution values for the intact full-length thioredoxin, confirming that the secondary structure is retained in the reassembled complex prepared as a poly(ethylene glycol) precipitate. The differential labeling of complementary thioredoxin fragments introduced in this work is expected to be beneficial for high-resolution structural studies of protein interfaces formed by protein assemblies by solid-state NMR spectroscopy. |
| doi_str_mv | 10.1021/ja0464589 |
| format | Article |
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Backbone dihedral angles and secondary structure predicted from the statistical analysis of 13C and 15N chemical shifts are in general agreement with solution values for the intact full-length thioredoxin, confirming that the secondary structure is retained in the reassembled complex prepared as a poly(ethylene glycol) precipitate. The differential labeling of complementary thioredoxin fragments introduced in this work is expected to be beneficial for high-resolution structural studies of protein interfaces formed by protein assemblies by solid-state NMR spectroscopy.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja0464589</identifier><identifier>PMID: 15600367</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Carbon Isotopes ; Escherichia coli Proteins - chemistry ; Fundamental and applied biological sciences. 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Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>De novo site-specific backbone and side-chain resonance assignments are presented for U-15N(1-73)/U-13C,15N(74-108) reassembly of Escherichia coli thioredoxin by fragment complementation, determined using solid-state magic angle spinning NMR spectroscopy at 17.6 T. Backbone dihedral angles and secondary structure predicted from the statistical analysis of 13C and 15N chemical shifts are in general agreement with solution values for the intact full-length thioredoxin, confirming that the secondary structure is retained in the reassembled complex prepared as a poly(ethylene glycol) precipitate. The differential labeling of complementary thioredoxin fragments introduced in this work is expected to be beneficial for high-resolution structural studies of protein interfaces formed by protein assemblies by solid-state NMR spectroscopy.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carbon Isotopes</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nitrogen Isotopes</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Peptide Fragments - chemistry</subject><subject>Polyethylene Glycols - chemistry</subject><subject>Proteins</subject><subject>Thioredoxins - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkcFu1DAQhiMEoqVw4AWQL3BLseMkTo7LdksrtaXdXRC3aGKPty6JvdiO1H1Q3gcvXeA0_-j_9M9oJsveMnrKaME-PgAt67Jq2mfZMasKmlesqJ9nx5TSIhdNzY-yVyE8pLYsGvYyO2JVTSmvxXH26xo2RpKZ3QxIVltjrbEbsnKDUfkqQkRyc71MBsroXZBuuyPaebKKfpJx8jAkOSmDgThNbr2LaCy5tBG9BonhlCwxOAtWIpmFYDZ2RBv_wGdGa_SpMzAMO7Kw3sh7VGQRUtlrA0SmPcj63jiPyj2m5CVCCDj2QwL7HTn3sNkHkrkbtwPuJUTj7OvshYYh4JtDPcm-ni_W84v86svny_nsKjeFEDEXXFWq5dD2tNCaa6pVKRhtmZKFgL6ism80U1BJXmrAkjNQteilFBUvuFL8JPvwlLv17ueEIXajCRKHASy6KXS1YKKhVZvAdwdw6kdU3dabEfyu-_uIBLw_ABAkDNqnk5nwn6u5oG1DE5c_cSZEfPzng_-RhnFRdevbVXfB726-332ad9_4b9glq-A</recordid><startdate>20041222</startdate><enddate>20041222</enddate><creator>MARULANDA, Dabeiba</creator><creator>TASAYCO, Maria Luisa</creator><creator>MCDERMOTT, Ann</creator><creator>CATALDI, Marcela</creator><creator>ARRIARAN, Vilma</creator><creator>POLENOVA, Tatyana</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>20041222</creationdate><title>Magic Angle Spinning Solid-State NMR Spectroscopy for Structural Studies of Protein Interfaces. Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation</title><author>MARULANDA, Dabeiba ; TASAYCO, Maria Luisa ; MCDERMOTT, Ann ; CATALDI, Marcela ; ARRIARAN, Vilma ; POLENOVA, Tatyana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i277t-73d5d93a9b02ff3f0fd471091dc27ab50cb8f1da5c34fae431ad67bcc75323dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carbon Isotopes</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nitrogen Isotopes</topic><topic>Nuclear Magnetic Resonance, Biomolecular - methods</topic><topic>Peptide Fragments - chemistry</topic><topic>Polyethylene Glycols - chemistry</topic><topic>Proteins</topic><topic>Thioredoxins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MARULANDA, Dabeiba</creatorcontrib><creatorcontrib>TASAYCO, Maria Luisa</creatorcontrib><creatorcontrib>MCDERMOTT, Ann</creatorcontrib><creatorcontrib>CATALDI, Marcela</creatorcontrib><creatorcontrib>ARRIARAN, Vilma</creatorcontrib><creatorcontrib>POLENOVA, Tatyana</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</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 the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MARULANDA, Dabeiba</au><au>TASAYCO, Maria Luisa</au><au>MCDERMOTT, Ann</au><au>CATALDI, Marcela</au><au>ARRIARAN, Vilma</au><au>POLENOVA, Tatyana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Magic Angle Spinning Solid-State NMR Spectroscopy for Structural Studies of Protein Interfaces. Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2004-12-22</date><risdate>2004</risdate><volume>126</volume><issue>50</issue><spage>16608</spage><epage>16620</epage><pages>16608-16620</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>De novo site-specific backbone and side-chain resonance assignments are presented for U-15N(1-73)/U-13C,15N(74-108) reassembly of Escherichia coli thioredoxin by fragment complementation, determined using solid-state magic angle spinning NMR spectroscopy at 17.6 T. Backbone dihedral angles and secondary structure predicted from the statistical analysis of 13C and 15N chemical shifts are in general agreement with solution values for the intact full-length thioredoxin, confirming that the secondary structure is retained in the reassembled complex prepared as a poly(ethylene glycol) precipitate. The differential labeling of complementary thioredoxin fragments introduced in this work is expected to be beneficial for high-resolution structural studies of protein interfaces formed by protein assemblies by solid-state NMR spectroscopy.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15600367</pmid><doi>10.1021/ja0464589</doi><tpages>13</tpages></addata></record> |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Carbon Isotopes Escherichia coli Proteins - chemistry Fundamental and applied biological sciences. Psychology General aspects, investigation methods Models, Molecular Molecular Sequence Data Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular - methods Peptide Fragments - chemistry Polyethylene Glycols - chemistry Proteins Thioredoxins - chemistry |
| title | Magic Angle Spinning Solid-State NMR Spectroscopy for Structural Studies of Protein Interfaces. Resonance Assignments of Differentially Enriched Escherichia coli Thioredoxin Reassembled by Fragment Complementation |
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