메뉴 건너뛰기




Volumn 11, Issue 11, 2005, Pages 1688-1700

Solution probing of metal ion binding by helix 27 from Escherichia coli 16S rRNA

Author keywords

Metal ion binding; NMR spectroscopy; Terbium footprinting; Time resolved fluorescence resonance energy transfer (tr FRET)

Indexed keywords

MAGNESIUM ION; METAL ION; RIBOSOME RNA; TERBIUM;

EID: 27144444288     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2940705     Document Type: Article
Times cited : (8)

References (60)
  • 1
    • 0346366808 scopus 로고    scopus 로고
    • Symmetric K+ and Mg2+ ion-binding sites in the 5S rRNA loop E inferred from molecular dynamics simulations
    • Auffinger, P., Bielecki, L., and Westhof, E. 2004. Symmetric K+ and Mg2+ ion-binding sites in the 5S rRNA loop E inferred from molecular dynamics simulations. J. Mol. Biol. 335: 555-571.
    • (2004) J. Mol. Biol. , vol.335 , pp. 555-571
    • Auffinger, P.1    Bielecki, L.2    Westhof, E.3
  • 2
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P.B., and Steitz, T.A. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289: 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 3
    • 1942489762 scopus 로고    scopus 로고
    • Study of the functional interaction of the 900 tetraloop of 16S ribosomal RNA with helix 24 within the bacterial ribosome
    • Belanger, F., Gagnon, M.G., Steinberg, S.V., Cunningham, P.R., and Brakier-Gingras, L. 2004. Study of the functional interaction of the 900 tetraloop of 16S ribosomal RNA with helix 24 within the bacterial ribosome. J. Mol. Biol. 338: 683-693.
    • (2004) J. Mol. Biol. , vol.338 , pp. 683-693
    • Belanger, F.1    Gagnon, M.G.2    Steinberg, S.V.3    Cunningham, P.R.4    Brakier-Gingras, L.5
  • 4
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen, D.E., Clemons Jr., W.M., Carter, A.P., Morgan-Warren, R.J., Wimberly, B.T., and Ramakrishnan, V. 2000. The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. Cell 103: 1143-1154.
    • (2000) Cell , vol.103 , pp. 1143-1154
    • Brodersen, D.E.1    Clemons Jr., W.M.2    Carter, A.P.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 6
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter, A.P., Clemons, W.M., Brodersen, D.E., Morgan-Warren, R.J., Wimberly, B.T., and Ramakrishnan, V. 2000. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407: 340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 7
    • 0024319347 scopus 로고
    • Probing the environment of lanthanide binding sites in yeast tRNA(Phe) by specific metal-ion-promoted cleavages
    • Ciesiolka, J., Marciniec, T., and Krzyzosiak, W. 1989. Probing the environment of lanthanide binding sites in yeast tRNA(Phe) by specific metal-ion-promoted cleavages. Eur. J. Biochem. 182: 445-450.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 445-450
    • Ciesiolka, J.1    Marciniec, T.2    Krzyzosiak, W.3
  • 9
    • 0030856333 scopus 로고    scopus 로고
    • Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain
    • Correll, C.C., Freeborn, B., Moore, P.B., and Steitz, T.A. 1997. Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain. Cell 91: 705-712.
    • (1997) Cell , vol.91 , pp. 705-712
    • Correll, C.C.1    Freeborn, B.2    Moore, P.B.3    Steitz, T.A.4
  • 10
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 12
    • 1242274330 scopus 로고    scopus 로고
    • A guide to ions and RNA structure
    • Draper, D.E. 2004. A guide to ions and RNA structure. RNA 10: 335-343.
    • (2004) RNA , vol.10 , pp. 335-343
    • Draper, D.E.1
  • 14
    • 0032501997 scopus 로고    scopus 로고
    • Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexammine binding, molecular modeling, and NMR spectroscopy
    • Gdaniec, Z., Sierzputowska-Gracz, H., and Theil, E.C. 1998. Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexammine binding, molecular modeling, and NMR spectroscopy. Biochemistry 37: 1505-1512.
    • (1998) Biochemistry , vol.37 , pp. 1505-1512
    • Gdaniec, Z.1    Sierzputowska-Gracz, H.2    Theil, E.C.3
  • 15
    • 0345299164 scopus 로고    scopus 로고
    • Solution structure and thermodynamics of a divalent metal ion binding site in an RNA pseudoknot
    • Gonzalez Jr., R.L. and Tinoco Jr., I. 1999. Solution structure and thermodynamics of a divalent metal ion binding site in an RNA pseudoknot. J. Mol. Biol. 289: 1267-1282.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1267-1282
    • Gonzalez Jr., R.L.1    Tinoco Jr., I.2
  • 16
    • 0027690254 scopus 로고
    • Measurement of amide proton exchange rates and NOEs with water in 13C/15N-enriched calcineurin B
    • Grzesiek, S. and Bax, A. 1993. Measurement of amide proton exchange rates and NOEs with water in 13C/15N-enriched calcineurin B. J. Biomol. NMR 3: 627-638.
    • (1993) J. Biomol. NMR , vol.3 , pp. 627-638
    • Grzesiek, S.1    Bax, A.2
  • 18
    • 0033731585 scopus 로고    scopus 로고
    • Use of terbium as a probe of tRNA tertiary structure and folding
    • Hargittai, M.R. and Musier-Forsyth, K. 2000. Use of terbium as a probe of tRNA tertiary structure and folding. RNA 6: 1672-1680.
    • (2000) RNA , vol.6 , pp. 1672-1680
    • Hargittai, M.R.1    Musier-Forsyth, K.2
  • 19
    • 3342878362 scopus 로고    scopus 로고
    • Probing RNA structure and metal-binding sites using terbium footprinting
    • 6.8
    • Harris, D.A. and Walter, N.G. 2003. Probing RNA structure and metal-binding sites using terbium footprinting. Curr. Protocols Nucleic Acid Chem. 6.8: 6.8.1-6.8.8.
    • (2003) Curr. Protocols Nucleic Acid Chem.
    • Harris, D.A.1    Walter, N.G.2
  • 20
    • 84889376932 scopus 로고    scopus 로고
    • Terbium(III) footprinting as a probe of RNA structure and metal-binding sites
    • (eds. R.K. Hartmann et al.), Wiley-VCH, Weinheim
    • _. 2005. Terbium(III) footprinting as a probe of RNA structure and metal-binding sites. In Handbook of RNA biochemistry (eds. R.K. Hartmann et al.), pp. 205-213. Wiley-VCH, Weinheim.
    • (2005) Handbook of RNA Biochemistry , pp. 205-213
  • 21
    • 3342915806 scopus 로고    scopus 로고
    • Terbium-mediated footprinting probes a catalytic conformational switch in the antigenomic hepatitis delta virus ribozyme
    • Harris, D.A., Tinsley, R.A., and Walter, N.G. 2004. Terbium-mediated footprinting probes a catalytic conformational switch in the antigenomic hepatitis delta virus ribozyme. J. Mol. Biol. 341: 389-403.
    • (2004) J. Mol. Biol. , vol.341 , pp. 389-403
    • Harris, D.A.1    Tinsley, R.A.2    Walter, N.G.3
  • 22
    • 0032532765 scopus 로고    scopus 로고
    • Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations
    • Hermann, T. and Westhof, E. 1998. Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations. Structure 6: 1303-1314.
    • (1998) Structure , vol.6 , pp. 1303-1314
    • Hermann, T.1    Westhof, E.2
  • 23
    • 8744245325 scopus 로고    scopus 로고
    • Dynamics inherent in helix 27 from Escherichia coli 16S ribosomal RNA
    • Hoerter, J.A., Lambert, M.N., Pereira, M.J., and Walter, N.G. 2004. Dynamics inherent in helix 27 from Escherichia coli 16S ribosomal RNA. Biochemistry 43: 14624-14636.
    • (2004) Biochemistry , vol.43 , pp. 14624-14636
    • Hoerter, J.A.1    Lambert, M.N.2    Pereira, M.J.3    Walter, N.G.4
  • 24
    • 0038001437 scopus 로고    scopus 로고
    • Trans-acting hepatitis δ virus ribozyme: Catalytic core and global structure are dependent on the 50 substrate sequence
    • Jeong, S., Sefcikova, J., Tinsley, R.A., Rueda, D., and Walter NG. 2003. Trans-acting hepatitis δ virus ribozyme: Catalytic core and global structure are dependent on the 50 substrate sequence. Biochemistry 42: 7727-7740.
    • (2003) Biochemistry , vol.42 , pp. 7727-7740
    • Jeong, S.1    Sefcikova, J.2    Tinsley, R.A.3    Rueda, D.4    Walter, N.G.5
  • 25
    • 0031570344 scopus 로고    scopus 로고
    • Solution structure of a metal-binding site in the major groove of RNA complexed with cobalt (III) hexammine
    • Kieft, J.S. and Tinoco Jr., I. 1997. Solution structure of a metal-binding site in the major groove of RNA complexed with cobalt (III) hexammine. Structure 5: 713-721.
    • (1997) Structure , vol.5 , pp. 713-721
    • Kieft, J.S.1    Tinoco Jr., I.2
  • 26
    • 4344569647 scopus 로고    scopus 로고
    • The contribution of metal ions to the structural stability of the large ribosomal subunit
    • Klein, D.J., Moore, P.B., and Steitz, T.A. 2004. The contribution of metal ions to the structural stability of the large ribosomal subunit. RNA 10: 1366-1379.
    • (2004) RNA , vol.10 , pp. 1366-1379
    • Klein, D.J.1    Moore, P.B.2    Steitz, T.A.3
  • 27
    • 0032582795 scopus 로고    scopus 로고
    • A common motif organizes the structure of multi-helix loops in 16 S and 23 S ribosomal RNAs
    • Leontis, N.B. and Westhof, E. 1998. A common motif organizes the structure of multi-helix loops in 16 S and 23 S ribosomal RNAs. J. Mol. Biol. 283: 571-583.
    • (1998) J. Mol. Biol. , vol.283 , pp. 571-583
    • Leontis, N.B.1    Westhof, E.2
  • 28
    • 0000751590 scopus 로고
    • Effects of chemical exchange on NMR spectra
    • (ed. G.C.K. Roberts), Oxford University Press, Oxford, UK
    • Lian, L.-Y. and Roberts, C. 1993. Effects of chemical exchange on NMR spectra. In NMR of macromolecules: A practical approach (ed. G.C.K. Roberts), pp. 153-181. Oxford University Press, Oxford, UK.
    • (1993) NMR of Macromolecules: A Practical Approach , pp. 153-181
    • Lian, L.-Y.1    Roberts, C.2
  • 29
    • 0030806152 scopus 로고    scopus 로고
    • A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA
    • Lodmell, J.S. and Dahlberg, A.E. 1997. A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA. Science 277: 1262-1267.
    • (1997) Science , vol.277 , pp. 1262-1267
    • Lodmell, J.S.1    Dahlberg, A.E.2
  • 30
    • 0028853679 scopus 로고
    • Genetic and comparative analyses reveal an alternative secondary structure in the region of nt 912 of Escherichia coli 16S rRNA
    • Lodmell, J.S., Gutell, R.R., and Dahlberg, A.E. 1995. Genetic and comparative analyses reveal an alternative secondary structure in the region of nt 912 of Escherichia coli 16S rRNA. Proc. Natl. Acad. Sci. 92: 10555-10559.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 10555-10559
    • Lodmell, J.S.1    Gutell, R.R.2    Dahlberg, A.E.3
  • 31
    • 0034682614 scopus 로고    scopus 로고
    • Metal interactions with a GAAA RNA tetraloop characterized by (31)P NMR and phosphorothioate substitutions
    • Maderia, M., Horton, T.E., and DeRose, V.J. 2000. Metal interactions with a GAAA RNA tetraloop characterized by (31)P NMR and phosphorothioate substitutions. Biochemistry 39: 8193-8200.
    • (2000) Biochemistry , vol.39 , pp. 8193-8200
    • Maderia, M.1    Horton, T.E.2    DeRose, V.J.3
  • 32
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning, G.S. 1978. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q. Rev. Biophys. 11: 179-246.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 33
    • 0024362326 scopus 로고
    • Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin 1 beta
    • Marion, D., Driscoll, P.C., Kay, L.E., Wingfield, P.T., Bax, A., Gronenborn, A.M., and Clore, G.M. 1989. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: Application to interleukin 1 beta. Biochemistry 28: 6150-6156.
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1    Driscoll, P.C.2    Kay, L.E.3    Wingfield, P.T.4    Bax, A.5    Gronenborn, A.M.6    Clore, G.M.7
  • 34
    • 0030799197 scopus 로고    scopus 로고
    • Enormously fast RNA hydrolysis by lanthanide(III) ions under physiological conditions: Eminent candidates for novel tools of biotechnology
    • Matsumura, K. and Komiyama, M. 1997. Enormously fast RNA hydrolysis by lanthanide(III) ions under physiological conditions: Eminent candidates for novel tools of biotechnology. J. Biochem. 122: 387-394.
    • (1997) J. Biochem. , vol.122 , pp. 387-394
    • Matsumura, K.1    Komiyama, M.2
  • 35
    • 0037051639 scopus 로고    scopus 로고
    • Sequestering of Eu(III) by a GAAA RNA tetraloop
    • Mundoma, C. and Greenbaum, N.L. 2002. Sequestering of Eu(III) by a GAAA RNA tetraloop. J. Am. Chem. Soc. 124: 3525-3532.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3525-3532
    • Mundoma, C.1    Greenbaum, N.L.2
  • 37
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle, J.M., Murphy, F.V., Tarry, M.J., and Ramakrishnan, V. 2002. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111: 721-732.
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 38
    • 0037154091 scopus 로고    scopus 로고
    • Reaction pathway of the trans-acting hepatitis delta virus ribozyme: A conformational change accompanies catalysis
    • Pereira, M.J., Harris, D.A., Rueda, D., and Walter, N.G. 2002. Reaction pathway of the trans-acting hepatitis delta virus ribozyme: A conformational change accompanies catalysis. Biochemistry 41: 730-740.
    • (2002) Biochemistry , vol.41 , pp. 730-740
    • Pereira, M.J.1    Harris, D.A.2    Rueda, D.3    Walter, N.G.4
  • 39
    • 6344252614 scopus 로고    scopus 로고
    • Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation
    • Peske, F., Savelsbergh, A., Katunin, V.I., Rodnina, M.V., and Wintermeyer, W. 2004. Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation. J. Mol. Biol. 343: 1183-1194.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1183-1194
    • Peske, F.1    Savelsbergh, A.2    Katunin, V.I.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 40
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 41
    • 12844258405 scopus 로고    scopus 로고
    • Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex
    • Reblova, K., Spackova, N., Koca, J., Leontis, N.B., and Sponer, J. 2004. Long-residency hydration, cation binding, and dynamics of loop E/helix IV rRNA-L25 protein complex. Biophys. J. 87: 3397-3412.
    • (2004) Biophys. J. , vol.87 , pp. 3397-3412
    • Reblova, K.1    Spackova, N.2    Koca, J.3    Leontis, N.B.4    Sponer, J.5
  • 42
    • 0346362326 scopus 로고    scopus 로고
    • Genetic evidence against the 16S ribosomal RNA helix 27 conformational switch model
    • Rodriguez-Correa, D. and Dahlberg, A.E. 2004. Genetic evidence against the 16S ribosomal RNA helix 27 conformational switch model. RNA 10: 28-33.
    • (2004) RNA , vol.10 , pp. 28-33
    • Rodriguez-Correa, D.1    Dahlberg, A.E.2
  • 43
    • 0034602926 scopus 로고    scopus 로고
    • Solution structure of cobalt(III)-hexammine complexed to the GAAA tetraloop, and metal-ion binding to G.A mismatches
    • Rudisser, S. and Tinoco Jr., I. 2000. Solution structure of cobalt(III)-hexammine complexed to the GAAA tetraloop, and metal-ion binding to G.A mismatches. J. Mol. Biol. 295: 1211-1223.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1211-1223
    • Rudisser, S.1    Tinoco Jr., I.2
  • 44
    • 0041972623 scopus 로고    scopus 로고
    • Diffusely bound Mg2+ ions slightly reorient stems I and II of the hammerhead ribozyme to increase the probability of formation of the catalytic core
    • Rueda, D., Wick, K., McDowell, S.E., and Walter, N.G. 2003. Diffusely bound Mg2+ ions slightly reorient stems I and II of the hammerhead ribozyme to increase the probability of formation of the catalytic core. Biochemistry 42: 9924-9936.
    • (2003) Biochemistry , vol.42 , pp. 9924-9936
    • Rueda, D.1    Wick, K.2    McDowell, S.E.3    Walter, N.G.4
  • 46
    • 0036224052 scopus 로고    scopus 로고
    • Effects of magnesium ions on the stabilization of RNA oligomers of defined structures
    • Serra, M.J., Baird, J.D., Dale, T., and Fey, B.L. 2002. Effects of magnesium ions on the stabilization of RNA oligomers of defined structures. RNA 8: 307-323.
    • (2002) RNA , vol.8 , pp. 307-323
    • Serra, M.J.1    Baird, J.D.2    Dale, T.3    Fey, B.L.4
  • 47
    • 0037530501 scopus 로고    scopus 로고
    • Lanthanide ions as probes for metal ions in the structure and catalytic mechanism of ribozymes
    • Sigel, R.K. and Pyle, A.M. 2003. Lanthanide ions as probes for metal ions in the structure and catalytic mechanism of ribozymes. Met. Ions Biol. Syst. 40: 477-512.
    • (2003) Met. Ions Biol. Syst. , vol.40 , pp. 477-512
    • Sigel, R.K.1    Pyle, A.M.2
  • 48
    • 0028953727 scopus 로고
    • The sarcin/ricin loop, a modular RNA
    • Szewczak, A.A. and Moore, P.B. 1995. The sarcin/ricin loop, a modular RNA. J. Mol. Biol. 247: 81-98.
    • (1995) J. Mol. Biol. , vol.247 , pp. 81-98
    • Szewczak, A.A.1    Moore, P.B.2
  • 49
    • 0042424707 scopus 로고    scopus 로고
    • Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy
    • Tama, F., Valle, M., Frank, J., and Brooks III, C.L. 2003. Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy. Proc. Natl. Acad. Sci. 100: 9319-9323.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 9319-9323
    • Tama, F.1    Valle, M.2    Frank, J.3    Brooks III, C.L.4
  • 50
    • 18544376661 scopus 로고    scopus 로고
    • Detection of RNA nucleobase metalation by NMR spectroscopy
    • Tanaka, Y. and Taira, K. 2005. Detection of RNA nucleobase metalation by NMR spectroscopy. Chem. Commun. (Camb.) 16: 2069-2079.
    • (2005) Chem. Commun. (Camb.) , vol.16 , pp. 2069-2079
    • Tanaka, Y.1    Taira, K.2
  • 51
    • 3142746008 scopus 로고    scopus 로고
    • Magnesium dependence of the amplified conformational switch in the trans-acting hepatitis delta virus ribozyme
    • Tinsley, R.A., Harris, D.A., and Walter, N.G. 2004. Magnesium dependence of the amplified conformational switch in the trans-acting hepatitis delta virus ribozyme. Biochemistry 43: 8935-8945.
    • (2004) Biochemistry , vol.43 , pp. 8935-8945
    • Tinsley, R.A.1    Harris, D.A.2    Walter, N.G.3
  • 54
    • 0032979707 scopus 로고    scopus 로고
    • Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction
    • Walter, N.G., Burke, J.M., and Millar, D.P. 1999. Stability of hairpin ribozyme tertiary structure is governed by the interdomain junction. Nat. Struct. Biol. 6: 544-549.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 544-549
    • Walter, N.G.1    Burke, J.M.2    Millar, D.P.3
  • 55
    • 0034607544 scopus 로고    scopus 로고
    • Probing non-selective cation binding in the hairpin ribozyme with Tb(III)
    • Walter, N.G., Yang, N., and Burke, J.M. 2000. Probing non-selective cation binding in the hairpin ribozyme with Tb(III). J. Mol. Biol. 298: 539-555.
    • (2000) J. Mol. Biol. , vol.298 , pp. 539-555
    • Walter, N.G.1    Yang, N.2    Burke, J.M.3
  • 56
    • 0041464604 scopus 로고    scopus 로고
    • Crystal structure of the leadzyme at 1.8 angstrom resolution: Metal ion binding and the implications for catalytic mechanism and allo site ion regulation
    • Wedekind, J.E. and McKay, D.B. 2003. Crystal structure of the leadzyme at 1.8 angstrom resolution: Metal ion binding and the implications for catalytic mechanism and allo site ion regulation. Biochemistry 42: 9554-9563.
    • (2003) Biochemistry , vol.42 , pp. 9554-9563
    • Wedekind, J.E.1    McKay, D.B.2
  • 57
    • 0001123057 scopus 로고
    • NMR of nucleic acids: From spectrum to structure
    • (ed. G.C.K. Roberts), Oxford University Press, Oxford, UK
    • Wijmenga, S., Mooren, M., and Hilbers, C. 1993. NMR of nucleic acids: From spectrum to structure. In NMR of macromolecules: A practical approach (ed. G.C.K. Roberts), pp. 217-288. Oxford University Press, Oxford, UK.
    • (1993) NMR of Macromolecules: A Practical Approach , pp. 217-288
    • Wijmenga, S.1    Mooren, M.2    Hilbers, C.3
  • 59
    • 16244363320 scopus 로고    scopus 로고
    • Metal ions and RNA folding: A highly charged topic with a dynamic future
    • Woodson, S.A. 2005. Metal ions and RNA folding: A highly charged topic with a dynamic future. Curr. Opin. Chem. Biol. 9: 104-109.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 104-109
    • Woodson, S.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.