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Volumn 107, Issue 12, 2014, Pages 2881-2890

Capturing Transition Paths and Transition States for Conformational Rearrangements in the Ribosome

Author keywords

[No Author keywords available]

Indexed keywords

TRANSFER RNA;

EID: 84920118389     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.10.022     Document Type: Article
Times cited : (41)

References (66)
  • 3
    • 80053391759 scopus 로고    scopus 로고
    • Capturing the essence of folding and functions of biomolecules using coarse-grained models
    • C. Hyeon, and D. Thirumalai Capturing the essence of folding and functions of biomolecules using coarse-grained models Nat. Commun. 2 2011 487
    • (2011) Nat. Commun. , vol.2 , pp. 487
    • Hyeon, C.1    Thirumalai, D.2
  • 4
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
    • B. Schuler, E.A. Lipman, and W.A. Eaton Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy Nature 419 2002 743 747
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 6
    • 36249028655 scopus 로고    scopus 로고
    • Single-molecule FRET with diffusion and conformational dynamics
    • I.V. Gopich, and A. Szabo Single-molecule FRET with diffusion and conformational dynamics J. Phys. Chem. B 111 2007 12925 12932
    • (2007) J. Phys. Chem. B , vol.111 , pp. 12925-12932
    • Gopich, I.V.1    Szabo, A.2
  • 7
    • 69949124663 scopus 로고    scopus 로고
    • Protein dynamics from single-molecule fluorescence intensity correlation functions
    • I.V. Gopich, and D. Nettels A. Szabo Protein dynamics from single-molecule fluorescence intensity correlation functions J. Chem. Phys. 131 2009 095102
    • (2009) J. Chem. Phys. , vol.131 , pp. 095102
    • Gopich, I.V.1    Nettels, D.2    Szabo, A.3
  • 8
    • 1642546396 scopus 로고    scopus 로고
    • Atomic simulations of protein folding, using the replica exchange algorithm
    • H. Nymeyer, S. Gnanakaran, and A.E. García Atomic simulations of protein folding, using the replica exchange algorithm Methods Enzymol. 383 2004 119 149
    • (2004) Methods Enzymol. , vol.383 , pp. 119-149
    • Nymeyer, H.1    Gnanakaran, S.2    García, A.E.3
  • 10
    • 79953747234 scopus 로고    scopus 로고
    • Cooperativity, local-nonlocal coupling, and nonnative interactions: Principles of protein folding from coarse-grained models
    • H.S. Chan, and Z. Zhang Z. Liu Cooperativity, local-nonlocal coupling, and nonnative interactions: principles of protein folding from coarse-grained models Annu. Rev. Phys. Chem. 62 2011 301 326
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 301-326
    • Chan, H.S.1    Zhang, Z.2    Liu, Z.3
  • 11
    • 84871375244 scopus 로고    scopus 로고
    • Transition paths, diffusive processes, and preequilibria of protein folding
    • Z. Zhang, and H.S. Chan Transition paths, diffusive processes, and preequilibria of protein folding Proc. Natl. Acad. Sci. USA 109 2012 20919 20924
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 20919-20924
    • Zhang, Z.1    Chan, H.S.2
  • 12
    • 78650049311 scopus 로고    scopus 로고
    • Overlap between folding and functional energy landscapes for adenylate kinase conformational change
    • U. Olsson, and M. Wolf-Watz Overlap between folding and functional energy landscapes for adenylate kinase conformational change Nat. Commun. 1 2010 111
    • (2010) Nat. Commun. , vol.1 , pp. 111
    • Olsson, U.1    Wolf-Watz, M.2
  • 13
    • 77951270272 scopus 로고    scopus 로고
    • Large conformational changes in proteins: Signaling and other functions
    • B.J. Grant, A.A. Gorfe, and J.A. McCammon Large conformational changes in proteins: signaling and other functions Curr. Opin. Struct. Biol. 20 2010 142 147
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 142-147
    • Grant, B.J.1    Gorfe, A.A.2    McCammon, J.A.3
  • 14
    • 0000359208 scopus 로고
    • Kinetic proofreading: A new mechanism for reducing errors in biosynthetic processes requiring high specificity
    • J.J. Hopfield Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity Proc. Natl. Acad. Sci. USA 71 1974 4135 4139
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4135-4139
    • Hopfield, J.J.1
  • 15
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • T. Pape, W. Wintermeyer, and M. Rodnina Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome EMBO J. 18 1999 3800 3807
    • (1999) EMBO J. , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 16
    • 0036646535 scopus 로고    scopus 로고
    • Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process
    • M. Valle, and J. Sengupta J. Frank Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process EMBO J. 21 2002 3557 3567
    • (2002) EMBO J. , vol.21 , pp. 3557-3567
    • Valle, M.1    Sengupta, J.2    Frank, J.3
  • 17
    • 0242407184 scopus 로고    scopus 로고
    • Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
    • M. Valle, and A. Zavialov J. Frank Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy Nat. Struct. Biol. 10 2003 899 906
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 899-906
    • Valle, M.1    Zavialov, A.2    Frank, J.3
  • 18
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • T.M. Schmeing, and V. Ramakrishnan What recent ribosome structures have revealed about the mechanism of translation Nature 461 2009 1234 1242
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 19
    • 84859593945 scopus 로고    scopus 로고
    • A new understanding of the decoding principle on the ribosome
    • N. Demeshkina, and L. Jenner G. Yusupova A new understanding of the decoding principle on the ribosome Nature 484 2012 256 259
    • (2012) Nature , vol.484 , pp. 256-259
    • Demeshkina, N.1    Jenner, L.2    Yusupova, G.3
  • 20
    • 42049086762 scopus 로고    scopus 로고
    • Rate and accuracy of bacterial protein synthesis revisited
    • M. Johansson, M. Lovmar, and M. Ehrenberg Rate and accuracy of bacterial protein synthesis revisited Curr. Opin. Microbiol. 11 2008 141 147
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 141-147
    • Johansson, M.1    Lovmar, M.2    Ehrenberg, M.3
  • 21
    • 79953159145 scopus 로고    scopus 로고
    • Distortion of tRNA upon near-cognate codon recognition on the ribosome
    • J. Mittelstaet, A.L. Konevega, and M.V. Rodnina Distortion of tRNA upon near-cognate codon recognition on the ribosome J. Biol. Chem. 286 2011 8158 8164
    • (2011) J. Biol. Chem. , vol.286 , pp. 8158-8164
    • Mittelstaet, J.1    Konevega, A.L.2    Rodnina, M.V.3
  • 23
    • 77954814800 scopus 로고    scopus 로고
    • Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome
    • P. Geggier, and R. Dave S.C. Blanchard Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome J. Mol. Biol. 399 2010 576 595
    • (2010) J. Mol. Biol. , vol.399 , pp. 576-595
    • Geggier, P.1    Dave, R.2    Blanchard, S.C.3
  • 24
    • 27644502679 scopus 로고    scopus 로고
    • Simulating movement of tRNA into the ribosome during decoding
    • K.Y. Sanbonmatsu, S. Joseph, and C.-S. Tung Simulating movement of tRNA into the ribosome during decoding Proc. Natl. Acad. Sci. USA 102 2005 15854 15859
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15854-15859
    • Sanbonmatsu, K.Y.1    Joseph, S.2    Tung, C.-S.3
  • 25
    • 77952717308 scopus 로고    scopus 로고
    • Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways
    • P.C. Whitford, and P. Geggier K.Y. Sanbonmatsu Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways RNA 16 2010 1196 1204
    • (2010) RNA , vol.16 , pp. 1196-1204
    • Whitford, P.C.1    Geggier, P.2    Sanbonmatsu, K.Y.3
  • 26
    • 40849084990 scopus 로고    scopus 로고
    • Dynamics of recognition between tRNA and elongation factor Tu
    • J. Eargle, and A.A. Black Z. Luthey-Schulten Dynamics of recognition between tRNA and elongation factor Tu J. Mol. Biol. 377 2008 1382 1405
    • (2008) J. Mol. Biol. , vol.377 , pp. 1382-1405
    • Eargle, J.1    Black, A.A.2    Luthey-Schulten, Z.3
  • 27
    • 78650211733 scopus 로고    scopus 로고
    • Functional role of ribosomal signatures
    • K. Chen, and J. Eargle Z. Luthey-Schulten Functional role of ribosomal signatures Biophys. J. 99 2010 3930 3940
    • (2010) Biophys. J. , vol.99 , pp. 3930-3940
    • Chen, K.1    Eargle, J.2    Luthey-Schulten, Z.3
  • 28
    • 34249887127 scopus 로고    scopus 로고
    • The antibiotic viomycin traps the ribosome in an intermediate state of translocation
    • D.N. Ermolenko, and P.C. Spiegel H.F. Noller The antibiotic viomycin traps the ribosome in an intermediate state of translocation Nat. Struct. Mol. Biol. 14 2007 493 497
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 493-497
    • Ermolenko, D.N.1    Spiegel, P.C.2    Noller, H.F.3
  • 29
    • 42949126723 scopus 로고    scopus 로고
    • Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation
    • J. Fei, and P. Kosuri R.L. Gonzalez Jr. Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation Mol. Cell 30 2008 348 359
    • (2008) Mol. Cell , vol.30 , pp. 348-359
    • Fei, J.1    Kosuri, P.2    Gonzalez, Jr.R.L.3
  • 30
    • 76249114762 scopus 로고    scopus 로고
    • Spontaneous formation of the unlocked state of the ribosome is a multistep process
    • J.B. Munro, and R.B. Altman S.C. Blanchard Spontaneous formation of the unlocked state of the ribosome is a multistep process Proc. Natl. Acad. Sci. USA 107 2010 709 714
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 709-714
    • Munro, J.B.1    Altman, R.B.2    Blanchard, S.C.3
  • 31
    • 33847254454 scopus 로고    scopus 로고
    • Ultrafast dynamics of protein collapse from single-molecule photon statistics
    • D. Nettels, and I.V. Gopich B. Schuler Ultrafast dynamics of protein collapse from single-molecule photon statistics Proc. Natl. Acad. Sci. USA 104 2007 2655 2660
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2655-2660
    • Nettels, D.1    Gopich, I.V.2    Schuler, B.3
  • 32
    • 44949091394 scopus 로고    scopus 로고
    • Pulling direction as a reaction coordinate for the mechanical unfolding of single molecules
    • R.B. Best, and E. Paci O.K. Dudko Pulling direction as a reaction coordinate for the mechanical unfolding of single molecules J. Phys. Chem. B 112 2008 5968 5976
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5968-5976
    • Best, R.B.1    Paci, E.2    Dudko, O.K.3
  • 33
    • 81055126961 scopus 로고    scopus 로고
    • Locating the barrier for folding of single molecules under an external force
    • O.K. Dudko, T.G. Graham, and R.B. Best Locating the barrier for folding of single molecules under an external force Phys. Rev. Lett. 107 2011 208301
    • (2011) Phys. Rev. Lett. , vol.107 , pp. 208301
    • Dudko, O.K.1    Graham, T.G.2    Best, R.B.3
  • 34
    • 73949127174 scopus 로고    scopus 로고
    • Refolding dynamics of stretched biopolymers upon force quench
    • C. Hyeon, and G. Morrison D. Thirumalai Refolding dynamics of stretched biopolymers upon force quench Proc. Natl. Acad. Sci. USA 106 2009 20288 20293
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20288-20293
    • Hyeon, C.1    Morrison, G.2    Thirumalai, D.3
  • 35
    • 84887117718 scopus 로고    scopus 로고
    • Native contacts determine protein folding mechanisms in atomistic simulations
    • R.B. Best, G. Hummer, and W.A. Eaton Native contacts determine protein folding mechanisms in atomistic simulations Proc. Natl. Acad. Sci. USA 110 2013 17874 17879
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 17874-17879
    • Best, R.B.1    Hummer, G.2    Eaton, W.A.3
  • 36
    • 31444452031 scopus 로고    scopus 로고
    • P versus Q: Structural reaction coordinates capture protein folding on smooth landscapes
    • S.S. Cho, Y. Levy, and P.G. Wolynes P versus Q: structural reaction coordinates capture protein folding on smooth landscapes Proc. Natl. Acad. Sci. USA 103 2006 586 591
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 586-591
    • Cho, S.S.1    Levy, Y.2    Wolynes, P.G.3
  • 37
    • 52949137003 scopus 로고    scopus 로고
    • Diffusive reaction dynamics on invariant free energy profiles
    • S.V. Krivov, and M. Karplus Diffusive reaction dynamics on invariant free energy profiles Proc. Natl. Acad. Sci. USA 105 2008 13841 13846
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13841-13846
    • Krivov, S.V.1    Karplus, M.2
  • 38
    • 33745611125 scopus 로고    scopus 로고
    • Low-dimensional, free-energy landscapes of protein-folding reactions by nonlinear dimensionality reduction
    • P. Das, and M. Moll C. Clementi Low-dimensional, free-energy landscapes of protein-folding reactions by nonlinear dimensionality reduction Proc. Natl. Acad. Sci. USA 103 2006 9885 9890
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9885-9890
    • Das, P.1    Moll, M.2    Clementi, C.3
  • 39
    • 0042424707 scopus 로고    scopus 로고
    • Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy
    • F. Tama, and M. Valle C.L. Brooks 3rd Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy Proc. Natl. Acad. Sci. USA 100 2003 9319 9323
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9319-9323
    • Tama, F.1    Valle, M.2    Brooks, C.L.3
  • 40
    • 66149167201 scopus 로고    scopus 로고
    • Collective dynamics of the ribosomal tunnel revealed by elastic network modeling
    • O. Kurkcuoglu, and Z. Kurkcuoglu R.L. Jernigan Collective dynamics of the ribosomal tunnel revealed by elastic network modeling Proteins 75 2009 837 845
    • (2009) Proteins , vol.75 , pp. 837-845
    • Kurkcuoglu, O.1    Kurkcuoglu, Z.2    Jernigan, R.L.3
  • 41
    • 79953320021 scopus 로고    scopus 로고
    • Determination of reaction coordinates via locally scaled diffusion map
    • M.A. Rohrdanz, and W. Zheng C. Clementi Determination of reaction coordinates via locally scaled diffusion map J. Chem. Phys. 134 2011 124116
    • (2011) J. Chem. Phys. , vol.134 , pp. 124116
    • Rohrdanz, M.A.1    Zheng, W.2    Clementi, C.3
  • 42
    • 77954192001 scopus 로고    scopus 로고
    • How the diffusivity profile reduces the arbitrariness of protein folding free energies
    • M. Hinczewski, and Y. von Hansen R.R. Netz How the diffusivity profile reduces the arbitrariness of protein folding free energies J. Chem. Phys. 132 2010 245103
    • (2010) J. Chem. Phys. , vol.132 , pp. 245103
    • Hinczewski, M.1    Von Hansen, Y.2    Netz, R.R.3
  • 43
    • 84890168470 scopus 로고    scopus 로고
    • Energy barriers and driving forces in tRNA translocation through the ribosome
    • L.V. Bock, and C. Blau H. Grubmüller Energy barriers and driving forces in tRNA translocation through the ribosome Nat. Struct. Mol. Biol. 20 2013 1390 1396
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1390-1396
    • Bock, L.V.1    Blau, C.2    Grubmüller, H.3
  • 44
    • 0842311640 scopus 로고    scopus 로고
    • From transition paths to transition states and rate coefficients
    • G. Hummer From transition paths to transition states and rate coefficients J. Chem. Phys. 120 2004 516 523
    • (2004) J. Chem. Phys. , vol.120 , pp. 516-523
    • Hummer, G.1
  • 45
    • 18744387720 scopus 로고    scopus 로고
    • Reaction coordinates and rates from transition paths
    • R.B. Best, and G. Hummer Reaction coordinates and rates from transition paths Proc. Natl. Acad. Sci. USA 102 2005 6732 6737
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6732-6737
    • Best, R.B.1    Hummer, G.2
  • 46
    • 63449135082 scopus 로고    scopus 로고
    • An all-atom structure-based potential for proteins: Bridging minimal models with all-atom empirical forcefields
    • P.C. Whitford, and J.K. Noel J.N. Onuchic An all-atom structure-based potential for proteins: bridging minimal models with all-atom empirical forcefields Proteins 75 2009 430 441
    • (2009) Proteins , vol.75 , pp. 430-441
    • Whitford, P.C.1    Noel, J.K.2    Onuchic, J.N.3
  • 47
    • 77954276842 scopus 로고    scopus 로고
    • SMOG@ctbp: Simplified deployment of structure-based models in GROMACS
    • J.K. Noel, and P.C. Whitford J.N. Onuchic SMOG@ctbp: simplified deployment of structure-based models in GROMACS Nucleic Acids Res. 38 2010 W657 W661
    • (2010) Nucleic Acids Res. , vol.38 , pp. W657-W661
    • Noel, J.K.1    Whitford, P.C.2    Onuchic, J.N.3
  • 48
    • 77956340277 scopus 로고    scopus 로고
    • Structural rearrangements of the ribosome at the tRNA proofreading step
    • L. Jenner, and N. Demeshkina M. Yusupov Structural rearrangements of the ribosome at the tRNA proofreading step Nat. Struct. Mol. Biol. 17 2010 1072 1078
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1072-1078
    • Jenner, L.1    Demeshkina, N.2    Yusupov, M.3
  • 49
    • 84864212951 scopus 로고    scopus 로고
    • The Shadow map: A general contact definition for capturing the dynamics of biomolecular folding and function
    • J.K. Noel, P.C. Whitford, and J.N. Onuchic The Shadow map: a general contact definition for capturing the dynamics of biomolecular folding and function J. Phys. Chem. B 116 2012 8692 8702
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8692-8702
    • Noel, J.K.1    Whitford, P.C.2    Onuchic, J.N.3
  • 50
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • E. Lindahl, B. Hess, and D. van der Spoel GROMACS 3.0: a package for molecular simulation and trajectory analysis J. Mol. Model. 7 2001 306 317
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 51
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, and C. Kutzner E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 52
    • 84863522650 scopus 로고    scopus 로고
    • Biomolecular dynamics: Order-disorder transitions and energy landscapes
    • P.C. Whitford, K.Y. Sanbonmatsu, and J.N. Onuchic Biomolecular dynamics: order-disorder transitions and energy landscapes Rep. Prog. Phys. 75 2012 076601
    • (2012) Rep. Prog. Phys. , vol.75 , pp. 076601
    • Whitford, P.C.1    Sanbonmatsu, K.Y.2    Onuchic, J.N.3
  • 53
    • 14544282086 scopus 로고    scopus 로고
    • The role of tRNA as a molecular spring in decoding, accommodation, and peptidyl transfer
    • J. Frank, and J. Sengupta M. Ehrenberg The role of tRNA as a molecular spring in decoding, accommodation, and peptidyl transfer FEBS Lett. 579 2005 959 962
    • (2005) FEBS Lett. , vol.579 , pp. 959-962
    • Frank, J.1    Sengupta, J.2    Ehrenberg, M.3
  • 54
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited
    • H. Shi, and P.B. Moore The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: a classic structure revisited RNA 6 2000 1091 1105
    • (2000) RNA , vol.6 , pp. 1091-1105
    • Shi, H.1    Moore, P.B.2
  • 55
    • 77953652658 scopus 로고    scopus 로고
    • The crystal structure of unmodified tRNAPhe from Escherichia coli
    • R.T. Byrne, and A.L. Konevega A.A. Antson The crystal structure of unmodified tRNAPhe from Escherichia coli Nucleic Acids Res. 38 2010 4154 4162
    • (2010) Nucleic Acids Res. , vol.38 , pp. 4154-4162
    • Byrne, R.T.1    Konevega, A.L.2    Antson, A.A.3
  • 56
    • 77954650144 scopus 로고    scopus 로고
    • Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    • N. Fischer, and A.L. Konevega H. Stark Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy Nature 466 2010 329 333
    • (2010) Nature , vol.466 , pp. 329-333
    • Fischer, N.1    Konevega, A.L.2    Stark, H.3
  • 57
    • 73549106134 scopus 로고    scopus 로고
    • Natural amino acids do not require their native tRNAs for efficient selection by the ribosome
    • P.R. Effraim, and J. Wang V.W. Cornish Natural amino acids do not require their native tRNAs for efficient selection by the ribosome Nat. Chem. Biol. 5 2009 947 953
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 947-953
    • Effraim, P.R.1    Wang, J.2    Cornish, V.W.3
  • 59
    • 35348852506 scopus 로고    scopus 로고
    • The role of fluctuations in tRNA selection by the ribosome
    • T.-H. Lee, and S.C. Blanchard S. Chu The role of fluctuations in tRNA selection by the ribosome Proc. Natl. Acad. Sci. USA 104 2007 13661 13665
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 13661-13665
    • Lee, T.-H.1    Blanchard, S.C.2    Chu, S.3
  • 60
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • T.M. Schmeing, and R.M. Voorhees V. Ramakrishnan The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA Science 326 2009 688 694
    • (2009) Science , vol.326 , pp. 688-694
    • Schmeing, T.M.1    Voorhees, R.M.2    Ramakrishnan, V.3
  • 61
    • 84867021896 scopus 로고    scopus 로고
    • Auto- and cross-power spectral analysis of dual trap optical tweezer experiments using Bayesian inference
    • Y. von Hansen, and A. Mehlich R.R. Netz Auto- and cross-power spectral analysis of dual trap optical tweezer experiments using Bayesian inference Rev. Sci. Instrum. 83 2012 095116
    • (2012) Rev. Sci. Instrum. , vol.83 , pp. 095116
    • Von Hansen, Y.1    Mehlich, A.2    Netz, R.R.3
  • 62
    • 84875249565 scopus 로고    scopus 로고
    • From mechanical folding trajectories to intrinsic energy landscapes of biopolymers
    • M. Hinczewski, and J.C.M. Gebhardt D. Thirumalai From mechanical folding trajectories to intrinsic energy landscapes of biopolymers Proc. Natl. Acad. Sci. USA 110 2013 4500 4505
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 4500-4505
    • Hinczewski, M.1    Gebhardt, J.C.M.2    Thirumalai, D.3
  • 64
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy-model (with applications to protein folding)
    • J.D. Bryngelson, and P.G. Wolynes Intermediates and barrier crossing in a random energy-model (with applications to protein folding) J. Phys. Chem 93 1989 6902 6915
    • (1989) J. Phys. Chem , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 65
    • 77957159348 scopus 로고    scopus 로고
    • Connecting energy landscapes with experimental rates for aminoacyl-tRNA accommodation in the ribosome
    • P.C. Whitford, J.N. Onuchic, and K.Y. Sanbonmatsu Connecting energy landscapes with experimental rates for aminoacyl-tRNA accommodation in the ribosome J. Am. Chem. Soc. 132 2010 13170 13171
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13170-13171
    • Whitford, P.C.1    Onuchic, J.N.2    Sanbonmatsu, K.Y.3
  • 66
    • 56049118660 scopus 로고    scopus 로고
    • Yeast ribosomal protein L10 helps coordinate tRNA movement through the large subunit
    • A.N. Petrov, and A. Meskauskas J.D. Dinman Yeast ribosomal protein L10 helps coordinate tRNA movement through the large subunit Nucleic Acids Res. 36 2008 6187 6198
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6187-6198
    • Petrov, A.N.1    Meskauskas, A.2    Dinman, J.D.3


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