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Volumn 506, Issue 7488, 2014, Pages 334-338

Protein-guided RNA dynamics during early ribosome assembly

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; FLUORESCENCE RESONANCE ENERGY TRANSFER; KINETICS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN CONFORMATION; RIBOSOMAL PROTEINS; RIBOSOME SUBUNITS, SMALL, BACTERIAL; RNA, RIBOSOMAL, 16S; RNA-BINDING PROTEINS;

EID: 84894235917     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13039     Document Type: Article
Times cited : (128)

References (61)
  • 2
    • 0016369454 scopus 로고
    • Total reconstitution of functionally active 50S ribosomal subunitsfrom Escherichiacoli
    • Nierhaus, K. H. & Dohme, F. Total reconstitution of functionally active 50S ribosomal subunitsfrom Escherichiacoli. Proc. Natl Acad. Sci. USA 71, 4713-4717 (1974).
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4713-4717
    • Nierhaus, K.H.1    Dohme, F.2
  • 3
    • 0014693477 scopus 로고
    • Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30S ribosomes studied in vitro
    • Traub, P. & Nomura, M. Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30S ribosomes studied in vitro. J. Mol. Biol. 40, 391-413 (1969).
    • (1969) J. Mol. Biol. , vol.40 , pp. 391-413
    • Traub, P.1    Nomura, M.2
  • 4
    • 0024344098 scopus 로고
    • RNA-protein interactions in 30Sribosomal subunits:folding and function of 16SrRNA
    • Stern, S., Powers, T., Changchien, L. M. & Noller, H. F. RNA-protein interactions in 30Sribosomal subunits:folding and function of 16SrRNA. Science 244, 783-790 (1989).
    • (1989) Science , vol.244 , pp. 783-790
    • Stern, S.1    Powers, T.2    Changchien, L.M.3    Noller, H.F.4
  • 6
    • 84255189102 scopus 로고    scopus 로고
    • RNA folding pathways and the self-assembly of ribosomes
    • Woodson, S. A. RNA folding pathways and the self-assembly of ribosomes. Acc. Chem. Res. 44, 1312-1319 (2011).
    • (2011) Acc. Chem. Res. , vol.44 , pp. 1312-1319
    • Woodson, S.A.1
  • 7
    • 0033529972 scopus 로고    scopus 로고
    • Ligand-induced conformational changes observed in single RNA molecules
    • Ha, T. et al. Ligand-induced conformational changes observed in single RNA molecules. Proc. Natl Acad. Sci. USA 96, 9077-9082 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9077-9082
    • Ha, T.1
  • 8
    • 0030593036 scopus 로고    scopus 로고
    • Assembly of a ribonucleoprotein catalyst by tertiary structure capture
    • Weeks, K. M. & Cech, T. R. Assembly of a ribonucleoprotein catalyst by tertiary structure capture. Science 271, 345-348 (1996).
    • (1996) Science , vol.271 , pp. 345-348
    • Weeks, K.M.1    Cech, T.R.2
  • 9
    • 0029869019 scopus 로고    scopus 로고
    • A tyrosyl-tRNA synthetase protein induces tertiary folding of the group i intron catalytic core
    • Caprara, M. G., Mohr, G. & Lambowitz, A. M. A tyrosyl-tRNA synthetase protein induces tertiary folding of the group I intron catalytic core. J. Mol. Biol. 257, 512-531 (1996).
    • (1996) J. Mol. Biol. , vol.257 , pp. 512-531
    • Caprara, M.G.1    Mohr, G.2    Lambowitz, A.M.3
  • 10
    • 0034615759 scopus 로고    scopus 로고
    • Structure of the S15, S6, S18-rRNA complex: Assembly of the 30S ribosome central domain
    • Agalarov, S. C., Sridhar Prasad, G., Funke, P. M., Stout, C. D. & Williamson, J. R. Structure of the S15, S6, S18-rRNA complex: assembly of the 30S ribosome central domain. Science 288, 107-112 (2000).
    • (2000) Science , vol.288 , pp. 107-112
    • Agalarov, S.C.1    Sridhar Prasad, G.2    Funke, P.M.3    Stout, C.D.4    Williamson, J.R.5
  • 11
    • 0036785939 scopus 로고    scopus 로고
    • Induced structural changes of 7SL RNA during the assembly of human signal recognition particle
    • Kuglstatter, A., Oubridge, C. & Nagai, K. Induced structural changes of 7SL RNA during the assembly of human signal recognition particle. Nature Struct. Biol. 9, 740-744 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 740-744
    • Kuglstatter, A.1    Oubridge, C.2    Nagai, K.3
  • 12
    • 55249084867 scopus 로고    scopus 로고
    • Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly
    • Adilakshmi, T., Bellur, D. L. & Woodson, S. A. Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly. Nature 455, 1268-1272 (2008).
    • (2008) Nature , vol.455 , pp. 1268-1272
    • Adilakshmi, T.1    Bellur, D.L.2    Woodson, S.A.3
  • 13
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: Fluorescence resonanceenergy transfer betweenasingle donor andasingle acceptor
    • Ha, T. et al. Probing the interaction between two single molecules: fluorescence resonanceenergy transfer betweenasingle donor andasingle acceptor. Proc. Natl Acad. Sci. USA 93, 6264-6268 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6264-6268
    • Ha, T.1
  • 14
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • Talkington, M. W., Siuzdak, G. & Williamson, J. R. An assembly landscape for the 30S ribosomal subunit. Nature 438, 628-632 (2005).
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.1    Siuzdak, G.2    Williamson, J.R.3
  • 15
    • 0023688660 scopus 로고
    • Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7
    • Nowotny, V. & Nierhaus, K. H. Assembly of the 30S subunit from Escherichia coli ribosomes occurs via two assembly domains which are initiated by S4 and S7. Biochemistry 27, 7051-7055 (1988).
    • (1988) Biochemistry , vol.27 , pp. 7051-7055
    • Nowotny, V.1    Nierhaus, K.H.2
  • 16
    • 0023042840 scopus 로고
    • Localization of the binding site for protein S4 on16S ribosomalRNAbychemical andenzymatic probingand primer extension
    • Stern, S., Wilson, R. C. & Noller, H. F. Localization of the binding site for protein S4 on16S ribosomalRNAbychemical andenzymatic probingand primer extension. J. Mol. Biol. 192, 101-110 (1986).
    • (1986) J. Mol. Biol. , vol.192 , pp. 101-110
    • Stern, S.1    Wilson, R.C.2    Noller, H.F.3
  • 17
    • 64549145364 scopus 로고    scopus 로고
    • Aminimized rRNA-binding site for ribosomal protein S4 and its implications for 30S assembly
    • Bellur, D. L. & Woodson, S. A. Aminimized rRNA-binding site for ribosomal protein S4 and its implications for 30S assembly. Nucleic Acids Res. 37, 1886-1896 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1886-1896
    • Bellur, D.L.1    Woodson, S.A.2
  • 18
    • 0028800665 scopus 로고
    • A temperature-dependent conformational rearrangementinthe ribosomal protein S4.16S rRNA complex
    • Powers, T. & Noller, H. F. A temperature-dependent conformational rearrangementinthe ribosomal protein S4. 16S rRNA complex. J. Biol. Chem. 270, 1238-1242 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1238-1242
    • Powers, T.1    Noller, H.F.2
  • 19
    • 80052390494 scopus 로고    scopus 로고
    • Slow formation of stable complexes during coincubation of minimal rRNA and ribosomal protein S4
    • Mayerle, M., Bellur, D. L. & Woodson, S. A. Slow formation of stable complexes during coincubation of minimal rRNA and ribosomal protein S4. J. Mol. Biol. 412, 453-465 (2011).
    • (2011) J. Mol. Biol. , vol.412 , pp. 453-465
    • Mayerle, M.1    Bellur, D.L.2    Woodson, S.A.3
  • 20
    • 0025737972 scopus 로고
    • A functional pseudoknotin 16S ribosomal RNA
    • Powers, T. & Noller, H. F. A functional pseudoknotin 16S ribosomal RNA. EMBO J. 10, 2203-2214 (1991).
    • (1991) EMBO J. , vol.10 , pp. 2203-2214
    • Powers, T.1    Noller, H.F.2
  • 21
    • 64049105734 scopus 로고    scopus 로고
    • S16 throws a conformational switch during assembly of 30S 59 domain
    • Ramaswamy, P. & Woodson, S. A. S16 throws a conformational switch during assembly of 30S 59 domain. Nature Struct. Mol. Biol. 16, 438-445 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 438-445
    • Ramaswamy, P.1    Woodson, S.A.2
  • 22
    • 69349099213 scopus 로고    scopus 로고
    • Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20
    • Ramaswamy, P. & Woodson, S. A. Global stabilization of rRNA structure by ribosomal proteins S4, S17, and S20. J. Mol. Biol. 392, 666-677 (2009).
    • (2009) J. Mol. Biol. , vol.392 , pp. 666-677
    • Ramaswamy, P.1    Woodson, S.A.2
  • 23
    • 84868214921 scopus 로고    scopus 로고
    • The right angle (RA) motif:aprevalent ribosomal RNA structural pattern found ingroupIintrons
    • Grabow, W. W., Zhuang, Z., Swank, Z. N., Shea, J. E. & Jaeger, L. The right angle (RA) motif:aprevalent ribosomal RNA structural pattern found ingroupIintrons. J. Mol. Biol. 424, 54-67 (2012).
    • (2012) J. Mol. Biol. , vol.424 , pp. 54-67
    • Grabow, W.W.1    Zhuang, Z.2    Swank, Z.N.3    Shea, J.E.4    Jaeger, L.5
  • 24
    • 0034619497 scopus 로고    scopus 로고
    • Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy
    • Sayers, E. W., Gerstner, R. B., Draper, D. E. & Torchia, D. A. Structural preordering in the N-terminal region of ribosomal protein S4 revealed by heteronuclear NMR spectroscopy. Biochemistry 39, 13602-13613 (2000).
    • (2000) Biochemistry , vol.39 , pp. 13602-13613
    • Sayers, E.W.1    Gerstner, R.B.2    Draper, D.E.3    Torchia, D.A.4
  • 25
    • 0346500500 scopus 로고    scopus 로고
    • Conformational flexibility of four-way junctions in RNA
    • Hohng, S. et al. Conformational flexibility of four-way junctions in RNA. J. Mol. Biol. 336, 69-79 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 69-79
    • Hohng, S.1
  • 27
    • 0035912931 scopus 로고    scopus 로고
    • Recognition of 16S rRNA by ribosomal protein S4 from Bacillus stearothermophilus
    • Gerstner, R. B., Pak, Y. & Draper, D. E. Recognition of 16S rRNA by ribosomal protein S4 from Bacillus stearothermophilus. Biochemistry 40, 7165-7173 (2001).
    • (2001) Biochemistry , vol.40 , pp. 7165-7173
    • Gerstner, R.B.1    Pak, Y.2    Draper, D.E.3
  • 28
    • 84862271578 scopus 로고    scopus 로고
    • Assembly of the five-way junction in the ribosomal small subunit using hybrid MD-Go simulations
    • Chen, K. et al. Assembly of the five-way junction in the ribosomal small subunit using hybrid MD-Go simulations. J. Phys. Chem. B 116, 6819-6831 (2012).
    • (2012) J. Phys. Chem. B , vol.116 , pp. 6819-6831
    • Chen, K.1
  • 29
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • Zhuang, X. et al. Correlating structural dynamics and function in single ribozyme molecules. Science 296, 1473-1476 (2002).
    • (2002) Science , vol.296 , pp. 1473-1476
    • Zhuang, X.1
  • 30
    • 0043009768 scopus 로고    scopus 로고
    • A four-way junction accelerates hairpin ribozyme folding via adiscrete intermediate
    • Tan, E. et al. A four-way junction accelerates hairpin ribozyme folding via adiscrete intermediate. Proc. Natl Acad. Sci. USA 100, 9308-9313 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9308-9313
    • Tan, E.1
  • 31
    • 0347004715 scopus 로고    scopus 로고
    • Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme
    • Xie, Z., Srividya, N., Sosnick, T. R., Pan, T. & Scherer, N. F. Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme. Proc. Natl Acad. Sci. USA 101, 534-539 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 534-539
    • Xie, Z.1    Srividya, N.2    Sosnick, T.R.3    Pan, T.4    Scherer, N.F.5
  • 32
    • 58149083620 scopus 로고    scopus 로고
    • A rugged free energy landscape separates multiple functional RNA folds throughout denaturation
    • Ditzler, M. A., Rueda, D., Mo, J., Hakansson, K. & Walter, N. G. A rugged free energy landscape separates multiple functional RNA folds throughout denaturation. Nucleic Acids Res. 36, 7088-7099 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 7088-7099
    • Ditzler, M.A.1    Rueda, D.2    Mo, J.3    Hakansson, K.4    Walter, N.G.5
  • 33
    • 76249126156 scopus 로고    scopus 로고
    • Multiple native states reveal persistent ruggednessofanRNA folding landscape
    • Solomatin, S. V., Greenfeld, M., Chu, S. & Herschlag, D. Multiple native states reveal persistent ruggednessofanRNA folding landscape. Nature463, 681-684 (2010).
    • (2010) Nature , vol.463 , pp. 681-684
    • Solomatin, S.V.1    Greenfeld, M.2    Chu, S.3    Herschlag, D.4
  • 34
    • 84875043544 scopus 로고    scopus 로고
    • Folding and ligand recognition of the TPP riboswitch aptamer at single-molecule resolution
    • Haller, A., Altman, R. B., Souliere, M. F., Blanchard, S. C. & Micura, R. Folding and ligand recognition of the TPP riboswitch aptamer at single-molecule resolution. Proc. Natl Acad. Sci. USA 110, 4188-4193 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 4188-4193
    • Haller, A.1    Altman, R.B.2    Souliere, M.F.3    Blanchard, S.C.4    Micura, R.5
  • 35
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • Hohng, S., Joo, C. & Ha, T. Single-molecule three-color FRET. Biophys. J. 87, 1328-1337 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 37
    • 0032541335 scopus 로고    scopus 로고
    • The solution structure of ribosomal protein S4 D41 reveals two subdomains and a positively charged surface that may interact with RNA
    • Markus, M. A., Gerstner, R. B., Draper, D. E. & Torchia, D. A. The solution structure of ribosomal protein S4 D41 reveals two subdomains and a positively charged surface that may interact with RNA. EMBO J. 17, 4559-4571 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4559-4571
    • Markus, M.A.1    Gerstner, R.B.2    Draper, D.E.3    Torchia, D.A.4
  • 38
    • 0035007334 scopus 로고    scopus 로고
    • Visualizing induced fit in early assembly of the human signal recognition particle
    • Rose, M. A. & Weeks, K. M. Visualizing induced fit in early assembly of the human signal recognition particle. Nature Struct. Biol. 8, 515-520 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 515-520
    • Rose, M.A.1    Weeks, K.M.2
  • 39
    • 33947494652 scopus 로고    scopus 로고
    • Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein
    • Stone, M. D. et al. Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein. Nature 446, 458-461 (2007).
    • (2007) Nature , vol.446 , pp. 458-461
    • Stone, M.D.1
  • 40
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D. E. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl Acad. Sci. USA 44, 98-104 (1958).
    • (1958) Proc. Natl Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 41
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson, J. R. Induced fit in RNA-protein recognition. Nature Struct. Biol. 7, 834-837 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 42
    • 37549017736 scopus 로고    scopus 로고
    • Visualizing spatially correlated dynamics that directs RNA conformational transitions
    • Zhang, Q., Stelzer, A. C., Fisher, C. K. & Al-Hashimi, H. M. Visualizing spatially correlated dynamics that directs RNA conformational transitions. Nature 450, 1263-1267 (2007).
    • (2007) Nature , vol.450 , pp. 1263-1267
    • Zhang, Q.1    Stelzer, A.C.2    Fisher, C.K.3    Al-Hashimi, H.M.4
  • 43
    • 2942615089 scopus 로고    scopus 로고
    • The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit
    • Klein, D. J., Moore, P. B. & Steitz, T. A. The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. J. Mol. Biol. 340, 141-177 (2004).
    • (2004) J. Mol. Biol. , vol.340 , pp. 141-177
    • Klein, D.J.1    Moore, P.B.2    Steitz, T.A.3
  • 44
    • 33746793263 scopus 로고    scopus 로고
    • Two distinct binding modes of a protein cofactor with its target RNA
    • Bokinsky, G. et al. Two distinct binding modes of a protein cofactor with its target RNA. J. Mol. Biol. 361, 771-784 (2006).
    • (2006) J. Mol. Biol. , vol.361 , pp. 771-784
    • Bokinsky, G.1
  • 45
    • 84867663419 scopus 로고    scopus 로고
    • Intrinsic flexibility of snRNA hairpin loops facilitates protein binding
    • Rau, M., Stump, W. T. & Hall, K. B. Intrinsic flexibility of snRNA hairpin loops facilitates protein binding. RNA 18, 1984-1995 (2012).
    • (2012) RNA , vol.18 , pp. 1984-1995
    • Rau, M.1    Stump, W.T.2    Hall, K.B.3
  • 46
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • Boehr, D. D., Nussinov, R. & Wright, P. E. The role of dynamic conformational ensembles in biomolecular recognition. Nature Chem. Biol. 5, 789-796 (2009).
    • (2009) Nature Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 47
    • 0742322957 scopus 로고    scopus 로고
    • Mapping structural differences between 30S ribosomal subunit assembly intermediates
    • Holmes, K. L. & Culver, G. M. Mapping structural differences between 30S ribosomal subunit assembly intermediates. Nature Struct. Mol. Biol. 11, 179-186 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 179-186
    • Holmes, K.L.1    Culver, G.M.2
  • 48
    • 84888192078 scopus 로고    scopus 로고
    • In vivo X-ray footprinting of pre-30S ribosomes reveals chaperone-dependent remodeling of late assembly intermediates
    • Clatterbuck Soper, S. F., Dator, R. P., Limbach, P. A. & Woodson, S. A. In vivo X-ray footprinting of pre-30S ribosomes reveals chaperone-dependent remodeling of late assembly intermediates. Mol. Cell 52, 506-516 (2013).
    • (2013) Mol. Cell , vol.52 , pp. 506-516
    • Clatterbuck Soper, S.F.1    Dator, R.P.2    Limbach, P.A.3    Woodson, S.A.4
  • 49
    • 84875423497 scopus 로고    scopus 로고
    • Specific contacts between proteinS4 and ribosomal RNA are required at multiple stages of ribosome assembly
    • Mayerle, M. & Woodson, S. A. Specific contacts between proteinS4 and ribosomal RNA are required at multiple stages of ribosome assembly. RNA 19, 574-585 (2013).
    • (2013) RNA , vol.19 , pp. 574-585
    • Mayerle, M.1    Woodson, S.A.2
  • 50
    • 12844274892 scopus 로고    scopus 로고
    • Efficient fluorescence labelingofa large RNA through oligonucleotide hybridization
    • Smith, G. J., Sosnick, T. R., Scherer, N. F. & Pan, T. Efficient fluorescence labelingofa large RNA through oligonucleotide hybridization. RNA 11, 234-239 (2005).
    • (2005) RNA , vol.11 , pp. 234-239
    • Smith, G.J.1    Sosnick, T.R.2    Scherer, N.F.3    Pan, T.4
  • 51
    • 13744257300 scopus 로고    scopus 로고
    • Site-specific labeling of the ribosome for single-molecule spectroscopy
    • Dorywalska, M. et al. Site-specific labeling of the ribosome for single-molecule spectroscopy. Nucleic Acids Res. 33, 182-189 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. 182-189
    • Dorywalska, M.1
  • 52
    • 0033057324 scopus 로고    scopus 로고
    • Efficient reconstitutionof functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins
    • Culver, G. M. & Noller, H. F. Efficient reconstitutionof functional Escherichia coli 30S ribosomal subunits from a complete set of recombinant small subunit ribosomal proteins. RNA 5, 832-843 (1999).
    • (1999) RNA , vol.5 , pp. 832-843
    • Culver, G.M.1    Noller, H.F.2
  • 53
    • 23644434688 scopus 로고    scopus 로고
    • Measurement of internal movements within the 30S ribosomal subunit using Forster resonance energy transfer
    • Hickerson, R., Majumdar, Z. K., Baucom, A., Clegg, R. M. & Noller, H. F. Measurement of internal movements within the 30S ribosomal subunit using Forster resonance energy transfer. J. Mol. Biol. 354, 459-472 (2005).
    • (2005) J. Mol. Biol. , vol.354 , pp. 459-472
    • Hickerson, R.1    Majumdar, Z.K.2    Baucom, A.3    Clegg, R.M.4    Noller, H.F.5
  • 54
    • 84867034988 scopus 로고    scopus 로고
    • Preparing sample chambers for single-molecule FRET
    • Joo, C. & Ha, T. Preparing sample chambers for single-molecule FRET. Cold Spring Harb Protoc 2012, 1104-1108 (2012).
    • (2012) Cold Spring Harb Protoc , vol.2012 , pp. 1104-1108
    • Joo, C.1    Ha, T.2
  • 55
    • 84855273566 scopus 로고    scopus 로고
    • Opening-closing dynamics of the mitochondrial transcription pre-initiation complex
    • Kim, H., Tang, G. Q., Patel, S. S. & Ha, T. Opening-closing dynamics of the mitochondrial transcription pre-initiation complex. Nucleic Acids Res. 40, 371-380 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. 371-380
    • Kim, H.1    Tang, G.Q.2    Patel, S.S.3    Ha, T.4
  • 56
    • 78650272919 scopus 로고    scopus 로고
    • Single-molecule four-color FRET
    • Lee, J. et al. Single-molecule four-color FRET. Angew. Chem. Int. Edn Engl. 49, 9922-9925 (2010).
    • (2010) Angew. Chem. Int. Edn Engl. , vol.49 , pp. 9922-9925
    • Lee, J.1
  • 57
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 58
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • MacKerell, A. D., Jr, Banavali, N. & Foloppe, N. Development and current status of the CHARMM force field for nucleic acids. Biopolymers 56, 257-265 (2000).
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • MacKerell Jr., A.D.1    Banavali, N.2    Foloppe, N.3
  • 59
  • 60
    • 33947720028 scopus 로고    scopus 로고
    • Selective 29-hydroxyl acylation analyzed by primer extension (SHAPE): Quantitative RNA structure analysis at single nucleotide resolution
    • Wilkinson, K. A., Merino, E. J. & Weeks, K. M. Selective 29-hydroxyl acylation analyzed by primer extension (SHAPE): quantitative RNA structure analysis at single nucleotide resolution. Nature Protocols 1, 1610-1616 (2006).
    • (2006) Nature Protocols , vol.1 , pp. 1610-1616
    • Wilkinson, K.A.1    Merino, E.J.2    Weeks, K.M.3
  • 61
    • 22544466402 scopus 로고    scopus 로고
    • Protein-independent folding pathway of the 16S rRNA 59 domain
    • Adilakshmi, T., Ramaswamy, P. & Woodson, S. A. Protein-independent folding pathway of the 16S rRNA 59 domain. J. Mol. Biol. 351, 508-519 (2005).
    • (2005) J. Mol. Biol. , vol.351 , pp. 508-519
    • Adilakshmi, T.1    Ramaswamy, P.2    Woodson, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.