NMR study of isoleucine transfer RNA from Thermus thermophilus
An NMR and nuclear Overhauser effect (NOE) analysis of Thermus thermophilus tRNAIle1a is presented. This species contains modifications including s2T54 and s4U8 [Horie, N., Hara-Yokoyama, M., Yokoyama, S., Watanabe, K., Kuchino, Y., Nishimura, S., & Miyazawa, T. (1985) Biochemistry 24, 5711-5715...
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| Veröffentlicht in: | Biochemistry (Easton) 1986-04, Vol.25 (7), p.1529-1534 |
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| container_title | Biochemistry (Easton) |
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| creator | Choi, B. S Redfield, Alfred G |
| description | An NMR and nuclear Overhauser effect (NOE) analysis of Thermus thermophilus tRNAIle1a is presented. This species contains modifications including s2T54 and s4U8 [Horie, N., Hara-Yokoyama, M., Yokoyama, S., Watanabe, K., Kuchino, Y., Nishimura, S., & Miyazawa, T. (1985) Biochemistry 24, 5711-5715]. All the expected secondary and reverse Hoogsteen AU pairs were identified, with one possible exception. The general geometry of the T psi C loop is the same as the Escherichia coli species, and there is NOE evidence for an A9-UA12 triple. Preliminary measurements of solvent exchange rates of internally hydrogen-bonded bases suggest that this tRNA is more stable than previously studied E. coli and yeast tRNAs. |
| doi_str_mv | 10.1021/bi00355a010 |
| format | Article |
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S ; Redfield, Alfred G</creator><creatorcontrib>Choi, B. S ; Redfield, Alfred G</creatorcontrib><description>An NMR and nuclear Overhauser effect (NOE) analysis of Thermus thermophilus tRNAIle1a is presented. This species contains modifications including s2T54 and s4U8 [Horie, N., Hara-Yokoyama, M., Yokoyama, S., Watanabe, K., Kuchino, Y., Nishimura, S., & Miyazawa, T. (1985) Biochemistry 24, 5711-5715]. All the expected secondary and reverse Hoogsteen AU pairs were identified, with one possible exception. The general geometry of the T psi C loop is the same as the Escherichia coli species, and there is NOE evidence for an A9-UA12 triple. Preliminary measurements of solvent exchange rates of internally hydrogen-bonded bases suggest that this tRNA is more stable than previously studied E. coli and yeast tRNAs.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00355a010</identifier><identifier>PMID: 3635410</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Base Sequence ; Biological and medical sciences ; Fundamental and applied biological sciences. 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S</creatorcontrib><creatorcontrib>Redfield, Alfred G</creatorcontrib><title>NMR study of isoleucine transfer RNA from Thermus thermophilus</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>An NMR and nuclear Overhauser effect (NOE) analysis of Thermus thermophilus tRNAIle1a is presented. This species contains modifications including s2T54 and s4U8 [Horie, N., Hara-Yokoyama, M., Yokoyama, S., Watanabe, K., Kuchino, Y., Nishimura, S., & Miyazawa, T. (1985) Biochemistry 24, 5711-5715]. All the expected secondary and reverse Hoogsteen AU pairs were identified, with one possible exception. The general geometry of the T psi C loop is the same as the Escherichia coli species, and there is NOE evidence for an A9-UA12 triple. Preliminary measurements of solvent exchange rates of internally hydrogen-bonded bases suggest that this tRNA is more stable than previously studied E. coli and yeast tRNAs.</description><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Magnetic Resonance Spectroscopy - methods</subject><subject>Molecular biophysics</subject><subject>Nucleic Acid Conformation</subject><subject>RNA, Transfer, Amino Acyl - isolation & purification</subject><subject>Spectroscopy : techniques and spectras</subject><subject>Thermus - genetics</subject><subject>Thermus thermophilus</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P20AQhldVEQTKqWckHyp6qExnv70XJBpKQOIjStPzarNeC4Mdhx1bgn_PRokiDpV6mhm9z4xGDyFfKZxRYPTnogbgUjqg8ImMqGSQC2PkZzICAJUzo-CAHCI-pVGAFvtknysuBYUROb-_m2XYD-Vb1lVZjV0TBl8vQ9ZHt8QqxGx2f5FVsWuz-WOI7YBZv67d6rFuBvxC9irXYDje1iPy9-r3fHyd3z5MbsYXt7kTVPS5AOqYp6owHGgQXAQF0hsfFIdFGijTvGSSFYI7bWShFHeF1EaXYEohAz8ip5u7q9i9DAF729boQ9O4ZegGtFqlVaGL_4JUSE1FIRP4YwP62CHGUNlVrFsX3ywFu9ZqP2hN9Mn27LBoQ7ljtx5T_m2bO_SuqZI8X-MO00YxKdZYvsFq7MPrLnbx2SrNtbTz6Z_UXf5ifCrsJPHfN7zzaJ-6IS6T5H8--A6kWpcQ</recordid><startdate>19860408</startdate><enddate>19860408</enddate><creator>Choi, B. 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Psychology</topic><topic>Magnetic Resonance Spectroscopy - methods</topic><topic>Molecular biophysics</topic><topic>Nucleic Acid Conformation</topic><topic>RNA, Transfer, Amino Acyl - isolation & purification</topic><topic>Spectroscopy : techniques and spectras</topic><topic>Thermus - genetics</topic><topic>Thermus thermophilus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Choi, B. 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S</au><au>Redfield, Alfred G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NMR study of isoleucine transfer RNA from Thermus thermophilus</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1986-04-08</date><risdate>1986</risdate><volume>25</volume><issue>7</issue><spage>1529</spage><epage>1534</epage><pages>1529-1534</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>An NMR and nuclear Overhauser effect (NOE) analysis of Thermus thermophilus tRNAIle1a is presented. This species contains modifications including s2T54 and s4U8 [Horie, N., Hara-Yokoyama, M., Yokoyama, S., Watanabe, K., Kuchino, Y., Nishimura, S., & Miyazawa, T. (1985) Biochemistry 24, 5711-5715]. All the expected secondary and reverse Hoogsteen AU pairs were identified, with one possible exception. The general geometry of the T psi C loop is the same as the Escherichia coli species, and there is NOE evidence for an A9-UA12 triple. Preliminary measurements of solvent exchange rates of internally hydrogen-bonded bases suggest that this tRNA is more stable than previously studied E. coli and yeast tRNAs.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>3635410</pmid><doi>10.1021/bi00355a010</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 1986-04, Vol.25 (7), p.1529-1534 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76843478 |
| source | ACS Publications; MEDLINE |
| subjects | Base Sequence Biological and medical sciences Fundamental and applied biological sciences. Psychology Magnetic Resonance Spectroscopy - methods Molecular biophysics Nucleic Acid Conformation RNA, Transfer, Amino Acyl - isolation & purification Spectroscopy : techniques and spectras Thermus - genetics Thermus thermophilus |
| title | NMR study of isoleucine transfer RNA from Thermus thermophilus |
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