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Volumn 377, Issue 5, 2008, Pages 1382-1405

Dynamics of Recognition between tRNA and Elongation Factor Tu

Author keywords

elongation factor Tu; evolution; MM PBSA; molecular dynamics; tRNA

Indexed keywords

ELONGATION FACTOR TU; TRANSFER RNA;

EID: 40849084990     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.073     Document Type: Article
Times cited : (64)

References (76)
  • 2
    • 1842743704 scopus 로고    scopus 로고
    • Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA
    • Theobald-Dietrich A., Frugier M., Giege R., and Rudinger-Thirion J. Atypical archaeal tRNA pyrrolysine transcript behaves towards EF-Tu as a typical elongator tRNA. Nucleic Acids Res. 32 (2004) 1091-1096
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1091-1096
    • Theobald-Dietrich, A.1    Frugier, M.2    Giege, R.3    Rudinger-Thirion, J.4
  • 4
    • 0033081413 scopus 로고    scopus 로고
    • Cys-EF-Tu-GDPNP reveals general and specific features in the ternary complex in the tRNA
    • Cys-EF-Tu-GDPNP reveals general and specific features in the ternary complex in the tRNA. Structure 7 (1999) 143-156
    • (1999) Structure , vol.7 , pp. 143-156
    • Nissen, P.1    Thirup, S.2    Kjeldgaard, M.3    Nyborg, J.4
  • 5
    • 0019162933 scopus 로고
    • Unusual modification patterns in the transfer ribonucleic acids of archaebacteria
    • Gupta R., and Woese C.R. Unusual modification patterns in the transfer ribonucleic acids of archaebacteria. Curr. Microbiol. 4 (1980) 245-249
    • (1980) Curr. Microbiol. , vol.4 , pp. 245-249
    • Gupta, R.1    Woese, C.R.2
  • 6
    • 0024358140 scopus 로고
    • Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes
    • Iwabe N., Kuma K., Hasegawa M., Osawa S., and Miyata T. Evolutionary relationship of archaebacteria, eubacteria, and eukaryotes inferred from phylogenetic trees of duplicated genes. Proc. Natl Acad. Sci. USA 86 (1989) 9355-9359
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9355-9359
    • Iwabe, N.1    Kuma, K.2    Hasegawa, M.3    Osawa, S.4    Miyata, T.5
  • 7
    • 34548690780 scopus 로고    scopus 로고
    • Indirect readout of tRNA for aminoacylation
    • Perona J., and Hou Y. Indirect readout of tRNA for aminoacylation. Biochemistry 46 (2007) 10419-10432
    • (2007) Biochemistry , vol.46 , pp. 10419-10432
    • Perona, J.1    Hou, Y.2
  • 8
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • LaRiviere F.J., Wolfson A.D., and Uhlenbeck O.C. Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science 294 (2001) 165-168
    • (2001) Science , vol.294 , pp. 165-168
    • LaRiviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 9
    • 2442697841 scopus 로고    scopus 로고
    • The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid
    • Dale T., Sanderson L.E., and Uhlenbeck O.C. The affinity of elongation factor Tu for an aminoacyl-tRNA is modulated by the esterified amino acid. Biochemistry 43 (2004) 6159-6166
    • (2004) Biochemistry , vol.43 , pp. 6159-6166
    • Dale, T.1    Sanderson, L.E.2    Uhlenbeck, O.C.3
  • 10
    • 34248993209 scopus 로고    scopus 로고
    • The 51-63 base pair of tRNA confers specificity for binding by EF-Tu
    • Sanderson L.E., and Uhlenbeck O.C. The 51-63 base pair of tRNA confers specificity for binding by EF-Tu. RNA 13 (2007) 835-840
    • (2007) RNA , vol.13 , pp. 835-840
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 11
    • 32644447756 scopus 로고    scopus 로고
    • Post-transcriptional nucleotide modification and alternative folding of RNA
    • Helm M. Post-transcriptional nucleotide modification and alternative folding of RNA. Nucleic Acids Res. 34 (2006) 721-733
    • (2006) Nucleic Acids Res. , vol.34 , pp. 721-733
    • Helm, M.1
  • 12
    • 0019250651 scopus 로고
    • 4-Thiouridine triggers both growth delay induced by near-ultraviolet light and photoprotection
    • Thomas G., and Favre A. 4-Thiouridine triggers both growth delay induced by near-ultraviolet light and photoprotection. Eur. J. Biochem. 113 (1980) 67-74
    • (1980) Eur. J. Biochem. , vol.113 , pp. 67-74
    • Thomas, G.1    Favre, A.2
  • 14
    • 0031566427 scopus 로고    scopus 로고
    • RNA hydration: three nanoseconds of multiple molecular dynamics simulations of the solvated tRNA(Asp) anticodon hairpin
    • Auffinger P., and Westhof E. RNA hydration: three nanoseconds of multiple molecular dynamics simulations of the solvated tRNA(Asp) anticodon hairpin. J. Mol. Biol. 269 (1997) 326-341
    • (1997) J. Mol. Biol. , vol.269 , pp. 326-341
    • Auffinger, P.1    Westhof, E.2
  • 15
    • 0033935223 scopus 로고    scopus 로고
    • Pseudouridine in RNA: what, where, how, and why
    • Charette M., and Gray M.W. Pseudouridine in RNA: what, where, how, and why. IUBMB Life 49 (2000) 341-351
    • (2000) IUBMB Life , vol.49 , pp. 341-351
    • Charette, M.1    Gray, M.W.2
  • 16
    • 0029566314 scopus 로고
    • Stabilization of RNA stacking by pseudouridine
    • Davis D.R. Stabilization of RNA stacking by pseudouridine. Nucleic Acids Res. 23 (1995) 5020-5026
    • (1995) Nucleic Acids Res. , vol.23 , pp. 5020-5026
    • Davis, D.R.1
  • 17
    • 0036303671 scopus 로고    scopus 로고
    • Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe)
    • Cabello-Villegas J., Winkler M.E., and Nikonowicz E.P. Solution conformations of unmodified and A(37)N(6)-dimethylallyl modified anticodon stem-loops of Escherichia coli tRNA(Phe). J. Mol. Biol. 319 (2002) 1015-1034
    • (2002) J. Mol. Biol. , vol.319 , pp. 1015-1034
    • Cabello-Villegas, J.1    Winkler, M.E.2    Nikonowicz, E.P.3
  • 18
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L., Brock A., Herberich B., and Schultz P.G. Expanding the genetic code of Escherichia coli. Science 292 (2001) 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 19
    • 0027976415 scopus 로고
    • Discrimination against misacylated tRNA by chloroplast elongation factor Tu
    • Stanzel M., Schon A., and Sprinzl M. Discrimination against misacylated tRNA by chloroplast elongation factor Tu. Eur. J. Biochem. 219 (1994) 435-439
    • (1994) Eur. J. Biochem. , vol.219 , pp. 435-439
    • Stanzel, M.1    Schon, A.2    Sprinzl, M.3
  • 20
    • 0032573150 scopus 로고    scopus 로고
    • Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways
    • Becker H.D., and Kern D. Thermus thermophilus: a link in evolution of the tRNA-dependent amino acid amidation pathways. Proc. Natl Acad. Sci. USA 95 (1998) 12832-12837
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12832-12837
    • Becker, H.D.1    Kern, D.2
  • 21
    • 34250843749 scopus 로고    scopus 로고
    • Structural elements defining elongation factor Tu mediated suppression of codon ambiguity
    • Roy H., Becker H.D., Mazauric M.-H., and Kern D. Structural elements defining elongation factor Tu mediated suppression of codon ambiguity. Nucleic Acids Res. 35 (2007) 3420-3430
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3420-3430
    • Roy, H.1    Becker, H.D.2    Mazauric, M.-H.3    Kern, D.4
  • 22
    • 0040559883 scopus 로고    scopus 로고
    • Quality control mechanisms during translation
    • Ibba M., and Söll D. Quality control mechanisms during translation. Science 286 (1999) 1893-1897
    • (1999) Science , vol.286 , pp. 1893-1897
    • Ibba, M.1    Söll, D.2
  • 25
    • 0030711616 scopus 로고    scopus 로고
    • Molecular switch in signal transduction: reaction paths of the conformational changes in ras p21
    • Ma J., and Karplus M. Molecular switch in signal transduction: reaction paths of the conformational changes in ras p21. Proc. Natl Acad. Sci. USA 94 (1997) 11905-11910
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11905-11910
    • Ma, J.1    Karplus, M.2
  • 27
    • 0022086231 scopus 로고
    • Molecular-dynamics simulation of phenylalanine transfer RNA. II. Amplitudes, anisotropies, and anharmonicities of atomic motions
    • Prabhakaran M., Harvey S.C., and McCammon J.A. Molecular-dynamics simulation of phenylalanine transfer RNA. II. Amplitudes, anisotropies, and anharmonicities of atomic motions. Biopolymers 24 (1985) 1189-1204
    • (1985) Biopolymers , vol.24 , pp. 1189-1204
    • Prabhakaran, M.1    Harvey, S.C.2    McCammon, J.A.3
  • 28
    • 33747881376 scopus 로고    scopus 로고
    • Molecular dynamics simulations of RNA systems
    • Hartmann R.K., Bindereif A., Schön A., and Westhof E. (Eds), Wiley-VCH Verlag, Weinheim, Germany chapt. 34
    • Auffinger P., and Vaiana A. Molecular dynamics simulations of RNA systems. In: Hartmann R.K., Bindereif A., Schön A., and Westhof E. (Eds). Handbook of RNA Biochemistry (2005), Wiley-VCH Verlag, Weinheim, Germany 560-576 chapt. 34
    • (2005) Handbook of RNA Biochemistry , pp. 560-576
    • Auffinger, P.1    Vaiana, A.2
  • 29
    • 0036280718 scopus 로고    scopus 로고
    • Molecular dynamics applied to nucleic acids
    • Norberg J., and Nilsson L. Molecular dynamics applied to nucleic acids. Acc. Chem. Res. 35 (2002) 465-472
    • (2002) Acc. Chem. Res. , vol.35 , pp. 465-472
    • Norberg, J.1    Nilsson, L.2
  • 30
  • 31
    • 0032907143 scopus 로고    scopus 로고
    • Molecular dynamics simulations of solvated yeast tRNA(Asp)
    • Auffinger P., Louise-May S., and Westhof E. Molecular dynamics simulations of solvated yeast tRNA(Asp). Biophys. J. 76 (1999) 50-64
    • (1999) Biophys. J. , vol.76 , pp. 50-64
    • Auffinger, P.1    Louise-May, S.2    Westhof, E.3
  • 32
    • 1242274330 scopus 로고    scopus 로고
    • A guide to ions and RNA structure
    • Draper D.E. A guide to ions and RNA structure. RNA 10 (2004) 335-343
    • (2004) RNA , vol.10 , pp. 335-343
    • Draper, D.E.1
  • 33
    • 0032532765 scopus 로고    scopus 로고
    • Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations
    • Hermann T., and Westhof E. Exploration of metal ion binding sites in RNA folds by Brownian-dynamics simulations. Structure 6 (1998) 1303-1314
    • (1998) Structure , vol.6 , pp. 1303-1314
    • Hermann, T.1    Westhof, E.2
  • 34
    • 0031008575 scopus 로고    scopus 로고
    • On the calculation of binding free energies using continuum methods: application to MHC class I protein-peptide interactions
    • Froloff N., Windemuth A., and Honig B. On the calculation of binding free energies using continuum methods: application to MHC class I protein-peptide interactions. Protein Sci. 6 (1997) 1293-1301
    • (1997) Protein Sci. , vol.6 , pp. 1293-1301
    • Froloff, N.1    Windemuth, A.2    Honig, B.3
  • 35
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models
    • Kollman P.A., Massova I., Reyes C., Kuhn B., Huo S., Chong L., et al. Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Acc. Chem. Res. 33 (2000) 889-897
    • (2000) Acc. Chem. Res. , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5    Chong, L.6
  • 36
    • 0035913537 scopus 로고    scopus 로고
    • Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions
    • Rocchia W., Alexov E., and Honig B. Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions. J. Phys. Chem. B 105 (2001) 6507-6514
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6507-6514
    • Rocchia, W.1    Alexov, E.2    Honig, B.3
  • 38
    • 0034646574 scopus 로고    scopus 로고
    • Structure and thermodynamics of RNA-protein binding: using molecular dynamics and free energy analyses to calculate the free energies of binding and conformational change
    • Reyes C.M., and Kollman P.A. Structure and thermodynamics of RNA-protein binding: using molecular dynamics and free energy analyses to calculate the free energies of binding and conformational change. J. Mol. Biol. 297 (2000) 1145-1158
    • (2000) J. Mol. Biol. , vol.297 , pp. 1145-1158
    • Reyes, C.M.1    Kollman, P.A.2
  • 39
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes
    • Gohlke H., Kiel C., and Case D.A. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes. J. Mol. Biol. 330 (2003) 891-913
    • (2003) J. Mol. Biol. , vol.330 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 40
    • 33749442647 scopus 로고    scopus 로고
    • MultiSeq: unifying sequence and structure data for evolutionary analysis
    • Roberts E., Eargle J., Wright D., and Luthey-Schulten Z. MultiSeq: unifying sequence and structure data for evolutionary analysis. BMC Bioinf. 7 (2006) 382
    • (2006) BMC Bioinf. , vol.7 , pp. 382
    • Roberts, E.1    Eargle, J.2    Wright, D.3    Luthey-Schulten, Z.4
  • 42
    • 13844284979 scopus 로고    scopus 로고
    • Evolutionary profiles from the QR factorization of multiple sequence alignments
    • Sethi A., O'Donoghue P., and Luthey-Schulten Z. Evolutionary profiles from the QR factorization of multiple sequence alignments. Proc. Natl Acad. Sci. USA 102 (2005) 4045-4050
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4045-4050
    • Sethi, A.1    O'Donoghue, P.2    Luthey-Schulten, Z.3
  • 45
    • 0021153752 scopus 로고
    • Halobacterium volcanii tRNAs. Identification of 41 tRNAs covering all amino acids, and the sequences of 33 class I tRNAs
    • Gupta R. Halobacterium volcanii tRNAs. Identification of 41 tRNAs covering all amino acids, and the sequences of 33 class I tRNAs. J. Biol. Chem. 259 (1984) 9461-9471
    • (1984) J. Biol. Chem. , vol.259 , pp. 9461-9471
    • Gupta, R.1
  • 46
    • 0027291262 scopus 로고
    • Recognition of tRNA(Cys) by Escherichia coli cysteinyl-tRNA synthetase
    • Komatsoulis G.A., and Abelson J. Recognition of tRNA(Cys) by Escherichia coli cysteinyl-tRNA synthetase. Biochemistry 32 (1993) 7435-7444
    • (1993) Biochemistry , vol.32 , pp. 7435-7444
    • Komatsoulis, G.A.1    Abelson, J.2
  • 47
    • 0037133662 scopus 로고    scopus 로고
    • The tRNA specificity of Thermus thermophilus EF-Tu
    • Asahara H., and Uhlenbeck O.C. The tRNA specificity of Thermus thermophilus EF-Tu. Proc. Natl Acad. Sci. USA 99 (2002) 3499-3504
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3499-3504
    • Asahara, H.1    Uhlenbeck, O.C.2
  • 48
    • 4344685227 scopus 로고    scopus 로고
    • Global ribosome motions revealed with elastic network model
    • Wang Y., Rader A.J., Bahar I., and Jernigan R.L. Global ribosome motions revealed with elastic network model. J. Struct. Biol. 147 (2004) 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
  • 50
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen P., Hansen J., Ban N., Moore P.B., and Steitz T.A. The structural basis of ribosome activity in peptide bond synthesis. Science 289 (2000) 920-930
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 51
    • 67049156092 scopus 로고    scopus 로고
    • Ionic solvation in aqueous and nonaqueous solutions
    • Ohtaki H. Ionic solvation in aqueous and nonaqueous solutions. Monatsh. Chem. 132 (2001) 1237-1268
    • (2001) Monatsh. Chem. , vol.132 , pp. 1237-1268
    • Ohtaki, H.1
  • 52
    • 0032707625 scopus 로고    scopus 로고
    • Calculating the electrostatic properties of RNA provides new insights into molecular interactions and function
    • Chin K., Sharp K.A., Honig B., and Pyle A.M. Calculating the electrostatic properties of RNA provides new insights into molecular interactions and function. Nat. Struct. Biol. 6 (1999) 1055-1061
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1055-1061
    • Chin, K.1    Sharp, K.A.2    Honig, B.3    Pyle, A.M.4
  • 54
    • 0001351515 scopus 로고
    • Estimation of absolute and relative entropies of macromolecules using the covariance matrix
    • Schlitter J. Estimation of absolute and relative entropies of macromolecules using the covariance matrix. Chem. Phys. Lett. 215 (1993) 617-621
    • (1993) Chem. Phys. Lett. , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 55
    • 0017393059 scopus 로고
    • Ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA: an equilibrium study
    • Pingoud A., Urbanke C., Krauss G., Peters F., and Maass G. Ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA: an equilibrium study. Eur. J. Biochem. 78 (1977) 403-409
    • (1977) Eur. J. Biochem. , vol.78 , pp. 403-409
    • Pingoud, A.1    Urbanke, C.2    Krauss, G.3    Peters, F.4    Maass, G.5
  • 56
    • 3242876311 scopus 로고    scopus 로고
    • BLAST: at the core of a powerful and diverse set of sequence analysis tools
    • McGinnis S., and Madden T.L. BLAST: at the core of a powerful and diverse set of sequence analysis tools. Nucleic Acids Res. 32 (2004) W20-W25
    • (2004) Nucleic Acids Res. , vol.32
    • McGinnis, S.1    Madden, T.L.2
  • 60
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 13844266306 scopus 로고    scopus 로고
    • Evolutionary profiles derived from the QR factorization of multiple structural alignments gives an economy of information
    • O'Donoghue P., and Luthey-Schulten Z. Evolutionary profiles derived from the QR factorization of multiple structural alignments gives an economy of information. J. Mol. Biol. 346 (2005) 875-894
    • (2005) J. Mol. Biol. , vol.346 , pp. 875-894
    • O'Donoghue, P.1    Luthey-Schulten, Z.2
  • 63
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence
    • Lowe T.M., and Eddy S.R. tRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res. 25 (1997) 955-964
    • (1997) Nucleic Acids Res. , vol.25 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 65
    • 0348244547 scopus 로고    scopus 로고
    • All-atom empirical force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data
    • Foloppe N., and MacKerrell Jr. A.D. All-atom empirical force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data. J. Comput. Chem. 21 (2000) 86-104
    • (2000) J. Comput. Chem. , vol.21 , pp. 86-104
    • Foloppe, N.1    MacKerrell Jr., A.D.2
  • 66
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald: An N·log(N) method for Ewald sums in large systems. J. Chem. Phys. 89 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.89 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 68
    • 0033551859 scopus 로고    scopus 로고
    • Insights into editing from an Ile-tRNA synthetase structure with tRNAIle and mupirocin
    • Silvian L.F., Wang J., and Steitz T.A. Insights into editing from an Ile-tRNA synthetase structure with tRNAIle and mupirocin. Science 285 (1999) 1074-1077
    • (1999) Science , vol.285 , pp. 1074-1077
    • Silvian, L.F.1    Wang, J.2    Steitz, T.A.3
  • 69
    • 0008875663 scopus 로고
    • Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA
    • Quigley G.J., Teeter M.M., and Rich A. Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proc. Natl Acad. Sci. USA 75 (1978) 64-68
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 64-68
    • Quigley, G.J.1    Teeter, M.M.2    Rich, A.3
  • 70
    • 0016732394 scopus 로고
    • tRNA conformation and magnesium binding. A study of a yeast phenylalanine-specific tRNA by a fluorescent indicator and differential melting curves
    • Römer R., and Hach R. tRNA conformation and magnesium binding. A study of a yeast phenylalanine-specific tRNA by a fluorescent indicator and differential melting curves. Eur. J. Biochem. 55 (1975) 271-284
    • (1975) Eur. J. Biochem. , vol.55 , pp. 271-284
    • Römer, R.1    Hach, R.2
  • 71
    • 84988103838 scopus 로고
    • Empirical energy functions for energy minimization and dynamics of nucleic acids
    • Nilsson L., and Karplus M. Empirical energy functions for energy minimization and dynamics of nucleic acids. J. Comput. Chem. 7 (1986) 591-616
    • (1986) J. Comput. Chem. , vol.7 , pp. 591-616
    • Nilsson, L.1    Karplus, M.2
  • 74
    • 0034323089 scopus 로고    scopus 로고
    • Absolute entropies from molecular dynamics simulation trajectories
    • Schafer A., Mark A.E., and van Gunsteren W.F. Absolute entropies from molecular dynamics simulation trajectories. J. Chem. Phys. 113 (2000) 7809-7817
    • (2000) J. Chem. Phys. , vol.113 , pp. 7809-7817
    • Schafer, A.1    Mark, A.E.2    van Gunsteren, W.F.3
  • 75
    • 0035828630 scopus 로고    scopus 로고
    • On the calculation of entropy from covariance matrices of the atomic fluctuations
    • Anricrioaei I., and Karplus M. On the calculation of entropy from covariance matrices of the atomic fluctuations. J. Chem. Phys. 115 (2001) 6289-6292
    • (2001) J. Chem. Phys. , vol.115 , pp. 6289-6292
    • Anricrioaei, I.1    Karplus, M.2
  • 76
    • 33749172039 scopus 로고    scopus 로고
    • Software news and updates. Carma: a molecular dynamics analysis program
    • Glykos N.M. Software news and updates. Carma: a molecular dynamics analysis program. J. Comput. Chem. 27 (2006) 1765-1768
    • (2006) J. Comput. Chem. , vol.27 , pp. 1765-1768
    • Glykos, N.M.1


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