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Volumn 8, Issue 9, 2012, Pages 3384-3394

Coarse-grained structure-based model for RNA-protein complexes developed by fluctuation matching

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EID: 84866150179     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct300361j     Document Type: Article
Times cited : (40)

References (81)
  • 1
    • 77956755947 scopus 로고    scopus 로고
    • Ribonucleoprotein multimers and their functions
    • Bleichert, F.; Baserga, S. J. Ribonucleoprotein multimers and their functions Crit. Rev. Biochem. Mol. 2010, 45, 331-350
    • (2010) Crit. Rev. Biochem. Mol. , vol.45 , pp. 331-350
    • Bleichert, F.1    Baserga, S.J.2
  • 2
    • 84857080591 scopus 로고    scopus 로고
    • Functional complexity and regulation through RNA dynamics
    • Dethoff, E. A.; Chugh, J.; Mustoe, A. M.; Al-Hashimi, H. M. Functional complexity and regulation through RNA dynamics Nature 2012, 482, 322-330
    • (2012) Nature , vol.482 , pp. 322-330
    • Dethoff, E.A.1    Chugh, J.2    Mustoe, A.M.3    Al-Hashimi, H.M.4
  • 4
    • 80053391759 scopus 로고    scopus 로고
    • Capturing the essence of folding and functions of biomolecules using coarse-grained models
    • Hyeon, C.; Thirumalai, D. Capturing the essence of folding and functions of biomolecules using coarse-grained models Nat. Commun. 2011, 2, 487
    • (2011) Nat. Commun. , vol.2 , pp. 487
    • Hyeon, C.1    Thirumalai, D.2
  • 5
    • 84861773417 scopus 로고    scopus 로고
    • Coarse-grained molecular simulations of large biomolecules
    • Takada, S. Coarse-grained molecular simulations of large biomolecules Curr. Opin. Struct. Biol. 2012, 22, 130-137
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 130-137
    • Takada, S.1
  • 6
    • 0028338898 scopus 로고
    • Modeling large RNAs and ribonucleoprotein particles using molecular mechanics techniques
    • Malhotra, A.; Tan, R. K.; Harvey, S. C. Modeling large RNAs and ribonucleoprotein particles using molecular mechanics techniques Biophys. J. 1994, 66, 1777-1795
    • (1994) Biophys. J. , vol.66 , pp. 1777-1795
    • Malhotra, A.1    Tan, R.K.2    Harvey, S.C.3
  • 7
    • 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.; Brooks, C. L. Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 9319-9323
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9319-9323
    • Tama, F.1    Valle, M.2    Frank, J.3    Brooks, C.L.4
  • 8
    • 4344685227 scopus 로고    scopus 로고
    • Global ribosome motions revealed with elastic network model
    • Wang, Y.; Rader, A. J.; Bahar, I.; Jernigan, R. L. Global ribosome motions revealed with elastic network model J. Struct. Biol. 2004, 147, 302-314
    • (2004) J. Struct. Biol. , vol.147 , pp. 302-314
    • Wang, Y.1    Rader, A.J.2    Bahar, I.3    Jernigan, R.L.4
  • 10
    • 24144478280 scopus 로고    scopus 로고
    • Exploring global motions and correlations in the ribosome
    • Trylska, J.; Tozzini, V.; McCammon, J. A. Exploring global motions and correlations in the ribosome Biophys. J. 2005, 89, 1455-1463
    • (2005) Biophys. J. , vol.89 , pp. 1455-1463
    • Trylska, J.1    Tozzini, V.2    McCammon, J.A.3
  • 11
    • 27744512500 scopus 로고    scopus 로고
    • Comparison of tRNA motions in the free and ribosomal bound structures
    • Wang, Y.; Jernigan, R. L. Comparison of tRNA motions in the free and ribosomal bound structures Biophys. J. 2005, 89, 3399-3409
    • (2005) Biophys. J. , vol.89 , pp. 3399-3409
    • Wang, Y.1    Jernigan, R.L.2
  • 12
    • 37349039627 scopus 로고    scopus 로고
    • Low-resolution molecular dynamics simulations of the 30S ribosomal subunit
    • Cui, Q.; Tan, R. K.-Z.; Harvey, S. C.; Case, D. A. Low-resolution molecular dynamics simulations of the 30S ribosomal subunit Multiscale Model. Simul. 2006, 5, 1248-1263
    • (2006) Multiscale Model. Simul. , vol.5 , pp. 1248-1263
    • Cui, Q.1    Tan, R.K.-Z.2    Harvey, S.C.3    Case, D.A.4
  • 13
    • 33846193288 scopus 로고    scopus 로고
    • Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins
    • Hyeon, C.; Dima, R. I.; Thirumalai, D. Pathways and kinetic barriers in mechanical unfolding and refolding of RNA and proteins Structure 2006, 14, 1633-1645
    • (2006) Structure , vol.14 , pp. 1633-1645
    • Hyeon, C.1    Dima, R.I.2    Thirumalai, D.3
  • 14
    • 35548950310 scopus 로고    scopus 로고
    • Automated de novo prediction of native-like RNA tertiary structures
    • Das, R.; Baker, D. Automated de novo prediction of native-like RNA tertiary structures Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 14664-14669
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 14664-14669
    • Das, R.1    Baker, D.2
  • 15
    • 58149310718 scopus 로고    scopus 로고
    • The ribosome structure controls and directs mRNA entry, translocation and exit dynamics
    • Kurkcuoglu, O.; Doruker, P.; Sen, T. Z.; Kloczkowski, A.; Jernigan, R. L. The ribosome structure controls and directs mRNA entry, translocation and exit dynamics Phys. Biol. 2008, 5, 046005
    • (2008) Phys. Biol. , vol.5 , pp. 046005
    • Kurkcuoglu, O.1    Doruker, P.2    Sen, T.Z.3    Kloczkowski, A.4    Jernigan, R.L.5
  • 17
    • 44149101971 scopus 로고    scopus 로고
    • Ab initio RNA folding by discrete molecular dynamics: From structure prediction to folding mechanisms
    • Ding, F.; Sharma, S.; Chalasani, P.; Demidov, V. V.; Broude, N. E.; Dokholyan, N. V. Ab initio RNA folding by discrete molecular dynamics: from structure prediction to folding mechanisms RNA 2008, 14, 1164-1173
    • (2008) RNA , vol.14 , pp. 1164-1173
    • Ding, F.1    Sharma, S.2    Chalasani, P.3    Demidov, V.V.4    Broude, N.E.5    Dokholyan, N.V.6
  • 18
    • 58249111738 scopus 로고    scopus 로고
    • Coarse-grained modeling of large RNA molecules with knowledge-based potentials and structural filters
    • Jonikas, M. A.; Radmer, R. J.; Laederach, A.; Das, R.; Pearlman, S.; Herschlag, D.; Altman, R. B. Coarse-grained modeling of large RNA molecules with knowledge-based potentials and structural filters RNA 2009, 15, 189-199
    • (2009) RNA , vol.15 , pp. 189-199
    • Jonikas, M.A.1    Radmer, R.J.2    Laederach, A.3    Das, R.4    Pearlman, S.5    Herschlag, D.6    Altman, R.B.7
  • 19
    • 77958490892 scopus 로고    scopus 로고
    • Coarse-grained model for simulation of RNA three-dimensional structures
    • Xia, Z.; Gardner, D. P.; Gutell, R. R.; Ren, P. Coarse-grained model for simulation of RNA three-dimensional structures J. Phys. Chem. B 2010, 114, 13497-13506
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13497-13506
    • Xia, Z.1    Gardner, D.P.2    Gutell, R.R.3    Ren, P.4
  • 20
    • 77956746033 scopus 로고    scopus 로고
    • HiRE-RNA: A high resolution coarse-grained energy model for RNA
    • Pasquali, S.; Derreumaux, P. HiRE-RNA: a high resolution coarse-grained energy model for RNA J. Phys. Chem. B 2010, 114, 11957-11966
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11957-11966
    • Pasquali, S.1    Derreumaux, P.2
  • 21
    • 78149461723 scopus 로고    scopus 로고
    • Coarse-grained models to study dynamics of nanoscale biomolecules and their applications to the ribosome
    • Trylska, J. Coarse-grained models to study dynamics of nanoscale biomolecules and their applications to the ribosome J. Phys.: Condens. Matter 2010, 22, 453101
    • (2010) J. Phys.: Condens. Matter , vol.22 , pp. 453101
    • Trylska, J.1
  • 22
    • 78349248253 scopus 로고    scopus 로고
    • Coarse-graining RNA nanostructures for molecular dynamics simulations
    • Paliy, M.; Melnik, R.; Shapiro, B. A. Coarse-graining RNA nanostructures for molecular dynamics simulations Phys. Biol. 2010, 7, 036001
    • (2010) Phys. Biol. , vol.7 , pp. 036001
    • Paliy, M.1    Melnik, R.2    Shapiro, B.A.3
  • 23
    • 79956189724 scopus 로고    scopus 로고
    • Fully differentiable coarse-grained and all-atom knowledge-based potentials for RNA structure evaluation
    • Bernauer, J.; Huang, X.; Sim, a. Y. L.; Levitt, M. Fully differentiable coarse-grained and all-atom knowledge-based potentials for RNA structure evaluation RNA 2011, 17, 1066-1075
    • (2011) RNA , vol.17 , pp. 1066-1075
    • Bernauer, J.1    Huang, X.2    Sim, A.Y.L.3    Levitt, M.4
  • 24
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go, N. Theoretical studies of protein folding Annu. Rev. Biophys. Bioeng. 1983, 12, 183-210
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 25
    • 0028947257 scopus 로고
    • Funnels, pathways and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D.; Onuchic, J. N.; Socci, N. D.; Wolynes, P. G. Funnels, pathways and the energy landscape of protein folding: a synthesis Proteins 1995, 21, 167-195
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 26
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins
    • Clementi, C.; Nymeyer, H.; Onuchic, J. N. Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins J. Mol. Biol. 2000, 298, 937-953
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 27
    • 33645770731 scopus 로고    scopus 로고
    • Folding-based molecular simulations reveal mechanisms of the rotary motor F1-ATPase
    • Koga, N.; Takada, S. Folding-based molecular simulations reveal mechanisms of the rotary motor F1-ATPase Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 5367-5372
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5367-5372
    • Koga, N.1    Takada, S.2
  • 28
    • 33747065536 scopus 로고    scopus 로고
    • Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations
    • Okazaki, K.; Koga, N.; Takada, S.; Onuchic, J. N.; Wolynes, P. G. Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 11844-11849
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11844-11849
    • Okazaki, K.1    Koga, N.2    Takada, S.3    Onuchic, J.N.4    Wolynes, P.G.5
  • 31
    • 77249151455 scopus 로고    scopus 로고
    • Multiscale modeling of proteins
    • Tozzini, V. Multiscale modeling of proteins Acc. Chem. Res. 2010, 43, 220-230
    • (2010) Acc. Chem. Res. , vol.43 , pp. 220-230
    • Tozzini, V.1
  • 32
    • 33746606875 scopus 로고    scopus 로고
    • The multiscale challenge for biomolecular systems: Coarse-grained modeling
    • Chu, J.; Izveko, S.; Voth, G. A. The multiscale challenge for biomolecular systems: coarse-grained modeling Mol. Simul. 2006, 32, 211-218
    • (2006) Mol. Simul. , vol.32 , pp. 211-218
    • Chu, J.1    Izveko, S.2    Voth, G.A.3
  • 34
    • 0028094855 scopus 로고
    • A quantitative model of the Escherichia coli 16 S RNA in the 30 S ribosomal subunit
    • Malhotra, A.; Harvey, S. C. A quantitative model of the Escherichia coli 16 S RNA in the 30 S ribosomal subunit J. Mol. Biol. 1994, 240, 308-340
    • (1994) J. Mol. Biol. , vol.240 , pp. 308-340
    • Malhotra, A.1    Harvey, S.C.2
  • 35
    • 77956203531 scopus 로고    scopus 로고
    • Multiscale methods for protein folding simulations
    • Li, W.; Yoshii, H.; Hori, N.; Kameda, T.; Takada, S. Multiscale methods for protein folding simulations Methods 2010, 52, 106-114
    • (2010) Methods , vol.52 , pp. 106-114
    • Li, W.1    Yoshii, H.2    Hori, N.3    Kameda, T.4    Takada, S.5
  • 40
    • 26444598454 scopus 로고    scopus 로고
    • Protein-nucleic acid recognition: Statistical analysis of atomic interactions and influence of DNA structure
    • Lejeune, D.; Delsaux, N.; Charloteaux, B.; Thomas, A.; Brasseur, R. Protein-nucleic acid recognition: statistical analysis of atomic interactions and influence of DNA structure Proteins 2005, 61, 258-271
    • (2005) Proteins , vol.61 , pp. 258-271
    • Lejeune, D.1    Delsaux, N.2    Charloteaux, B.3    Thomas, A.4    Brasseur, R.5
  • 41
    • 78049347710 scopus 로고    scopus 로고
    • Chromatin ionic atmosphere analyzed by a mesoscale electrostatic approach
    • Gan, H. H.; Schlick, T. Chromatin ionic atmosphere analyzed by a mesoscale electrostatic approach Biophys. J. 2010, 99, 2587-2596
    • (2010) Biophys. J. , vol.99 , pp. 2587-2596
    • Gan, H.H.1    Schlick, T.2
  • 44
    • 0345983583 scopus 로고    scopus 로고
    • Leontis, N. B.; Santa-Lucia, J., Eds.; American Chemical Society: Washington, DC
    • Macke, T.; Case, D. A. In Molecular Modeling of Nucleic Acids; Leontis, N. B.; Santa-Lucia, J., Eds.; American Chemical Society: Washington, DC, 1998; pp 379-393.
    • (1998) Molecular Modeling of Nucleic Acids , pp. 379-393
    • MacKe, T.1    Case, D.A.2
  • 47
    • 0029082529 scopus 로고
    • Structure of the P1 helix from group i self-splicing introns
    • Allain, F. H.; Varani, G. Structure of the P1 helix from group I self-splicing introns J. Mol. Biol. 1995, 250, 333-353
    • (1995) J. Mol. Biol. , vol.250 , pp. 333-353
    • Allain, F.H.1    Varani, G.2
  • 48
    • 0030596092 scopus 로고    scopus 로고
    • A network of heterogeneous hydrogen bonds in GNRA tetraloops
    • Jucker, F. M.; Heus, H. A.; Yip, P. F.; Moors, E. H. M.; Pardi, A. A network of heterogeneous hydrogen bonds in GNRA tetraloops J. Mol. Biol. 1996, 264, 968-980
    • (1996) J. Mol. Biol. , vol.264 , pp. 968-980
    • Jucker, F.M.1    Heus, H.A.2    Yip, P.F.3    Moors, E.H.M.4    Pardi, A.5
  • 49
    • 0031591383 scopus 로고    scopus 로고
    • The structure of an RNA "kissing" hairpin complex of the HIV TAR hairpin loop and its complement
    • Chang, K.-Y.; Tinoco, I. The structure of an RNA "kissing" hairpin complex of the HIV TAR hairpin loop and its complement J. Mol. Biol. 1997, 269, 52-66
    • (1997) J. Mol. Biol. , vol.269 , pp. 52-66
    • Chang, K.-Y.1    Tinoco, I.2
  • 51
    • 0030476765 scopus 로고    scopus 로고
    • Capturing the structure of a catalytic RNA intermediate: The hammerhead ribozyme
    • Scott, W. G.; Murray, J. B.; Arnold, J. R. P.; Stoddard, B. L.; Klug, A. Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme Science 1996, 274, 2065-2069
    • (1996) Science , vol.274 , pp. 2065-2069
    • Scott, W.G.1    Murray, J.B.2    Arnold, J.R.P.3    Stoddard, B.L.4    Klug, A.5
  • 52
    • 0033010932 scopus 로고    scopus 로고
    • Minor groove RNA triplex in the crystal structure of a ribosomal frameshifting viral pseudoknot
    • Su, L.; Chen, L.; Egli, M.; Berger, J. M.; Rich, A. Minor groove RNA triplex in the crystal structure of a ribosomal frameshifting viral pseudoknot Nat. Struct. Mol. Biol. 1999, 6, 285-292
    • (1999) Nat. Struct. Mol. Biol. , vol.6 , pp. 285-292
    • Su, L.1    Chen, L.2    Egli, M.3    Berger, J.M.4    Rich, A.5
  • 53
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited
    • Shi, H.; Moore, P. B. The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited RNA 2000, 6, 1091-1105
    • (2000) RNA , vol.6 , pp. 1091-1105
    • Shi, H.1    Moore, P.B.2
  • 54
    • 36248966494 scopus 로고    scopus 로고
    • The 1.3Å resolution structure of the RNA tridecamer r(GCGUUUGAAACGC): Metal ion binding correlates with base unstacking and groove contraction
    • Timsit, Y.; Bombard, S. The 1.3Å resolution structure of the RNA tridecamer r(GCGUUUGAAACGC): Metal ion binding correlates with base unstacking and groove contraction RNA 2007, 13, 2098-2107
    • (2007) RNA , vol.13 , pp. 2098-2107
    • Timsit, Y.1    Bombard, S.2
  • 55
    • 53049094260 scopus 로고    scopus 로고
    • Crystal structure of the lysine riboswitch regulatory mRNA element
    • Garst, A. D.; Héroux, A.; Rambo, R. P.; Batey, R. T. Crystal structure of the lysine riboswitch regulatory mRNA element J. Biol. Chem. 2008, 283, 22347-22351
    • (2008) J. Biol. Chem. , vol.283 , pp. 22347-22351
    • Garst, A.D.1    Héroux, A.2    Rambo, R.P.3    Batey, R.T.4
  • 56
    • 77956495754 scopus 로고    scopus 로고
    • Inclusion of weak high-resolution X-ray data for improvement of a group II intron structure
    • Wang, J. Inclusion of weak high-resolution X-ray data for improvement of a group II intron structure Acta Crystallogr., Sect. D 2010, 66, 988-1000
    • (2010) Acta Crystallogr., Sect. D , vol.66 , pp. 988-1000
    • Wang, J.1
  • 59
    • 0033553625 scopus 로고    scopus 로고
    • Crystal structure of a conserved ribosomal protein-RNA complex
    • Conn, G. L.; Draper, D. E.; Lattman, E. E.; Gittis, A. G. Crystal structure of a conserved ribosomal protein-RNA complex Science 1999, 284, 1171-1174
    • (1999) Science , vol.284 , pp. 1171-1174
    • Conn, G.L.1    Draper, D.E.2    Lattman, E.E.3    Gittis, A.G.4
  • 63
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge, C.; Ito, N.; Evans, P. R.; Teo, C.-H.; Nagai, K. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin Nature 1994, 372, 432-438
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.R.3    Teo, C.-H.4    Nagai, K.5
  • 64
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang, X.; Hall, T. M. T. Structural basis for recognition of AU-rich element RNA by the HuD protein Nat. Struct. Biol. 2001, 8, 141-145
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 141-145
    • Wang, X.1    Hall, T.M.T.2
  • 65
    • 0035913989 scopus 로고    scopus 로고
    • Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
    • Wild, K.; Sinning, I.; Cusack, S. Crystal structure of an early protein-RNA assembly complex of the signal recognition particle Science 2001, 294, 598-601
    • (2001) Science , vol.294 , pp. 598-601
    • Wild, K.1    Sinning, I.2    Cusack, S.3
  • 66
    • 0037071839 scopus 로고    scopus 로고
    • Structure of the SRP19-RNA complex and implications for signal recognition particle assembly
    • Hainzl, T.; Huang, S.; Sauer-Eriksson, A. E. Structure of the SRP19-RNA complex and implications for signal recognition particle assembly Nature 2002, 417, 767-771
    • (2002) Nature , vol.417 , pp. 767-771
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 68
    • 77951974177 scopus 로고    scopus 로고
    • Structural aspects of messenger RNA reading frame maintenance by the ribosome
    • Jenner, L.; Demeshkina, N.; Yusupova, G.; Yusupov, M. Structural aspects of messenger RNA reading frame maintenance by the ribosome Nat. Struct. Mol. Biol. 2010, 17, 555-560
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 555-560
    • Jenner, L.1    Demeshkina, N.2    Yusupova, G.3    Yusupov, M.4
  • 69
    • 34250318638 scopus 로고    scopus 로고
    • Refinement of the AMBER force field for nucleic acids: Improving the description of alpha/gamma conformers
    • Pérez, A.; Marchán, I.; Svozil, D.; Sponer, J.; Cheatham, T. E.; Laughton, C. a.; Orozco, M. Refinement of the AMBER force field for nucleic acids: improving the description of alpha/gamma conformers Biophys. J. 2007, 92, 3817-3829
    • (2007) Biophys. J. , vol.92 , pp. 3817-3829
    • Pérez, A.1    Marchán, I.2    Svozil, D.3    Sponer, J.4    Cheatham, T.E.5    A, L.C.6    Orozco, M.7
  • 70
    • 0344796204 scopus 로고
    • Ion-water interaction potentials derived from free energy perturbation simulations
    • Åqvist, J. Ion-water interaction potentials derived from free energy perturbation simulations J. Phys. Chem. 1990, 94, 8021-8024
    • (1990) J. Phys. Chem. , vol.94 , pp. 8021-8024
    • Åqvist, J.1
  • 74
    • 0028359395 scopus 로고
    • Dynamics of transfer RNAs analyzed by normal mode calculation
    • Nakamura, S.; Doi, J. Dynamics of transfer RNAs analyzed by normal mode calculation Nucleic Acids Res. 1994, 22, 514-521
    • (1994) Nucleic Acids Res. , vol.22 , pp. 514-521
    • Nakamura, S.1    Doi, J.2
  • 75
    • 79957906053 scopus 로고    scopus 로고
    • Examinations of tRNA range of motion using simulations of cryo-EM microscopy and X-ray data
    • Caulfield, T. R.; Devkota, B.; Rollins, G. C. Examinations of tRNA range of motion using simulations of cryo-EM microscopy and X-ray data J. Biophys. 2011, 2011, 219515
    • (2011) J. Biophys. , vol.2011 , pp. 219515
    • Caulfield, T.R.1    Devkota, B.2    Rollins, G.C.3
  • 78
    • 78149302861 scopus 로고    scopus 로고
    • The mechanism for activation of GTP hydrolysis on the ribosome
    • Voorhees, R.; Schmeing, T.; Kelley, A.; Ramakrishnan, V. The mechanism for activation of GTP hydrolysis on the ribosome Science 2010, 330, 835-838
    • (2010) Science , vol.330 , pp. 835-838
    • Voorhees, R.1    Schmeing, T.2    Kelley, A.3    Ramakrishnan, V.4
  • 81
    • 80555144942 scopus 로고    scopus 로고
    • A coarse-grain three-site-per-nucleotide model for DNA with explicit ions
    • Freeman, G. S.; Hinckley, D. M.; de Pablo, J. J. A coarse-grain three-site-per-nucleotide model for DNA with explicit ions J. Chem. Phys. 2011, 135, 165104
    • (2011) J. Chem. Phys. , vol.135 , pp. 165104
    • Freeman, G.S.1    Hinckley, D.M.2    De Pablo, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.