메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages 1536-1545

3D maps of RNA interhelical junctions

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; OXYGEN; PHOSPHATE;

EID: 80053394309     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2011.385     Document Type: Article
Times cited : (40)

References (60)
  • 1
    • 0030870075 scopus 로고    scopus 로고
    • Objectively judging the quality of a protein structure from a Ramachandran plot
    • Hooft, R.W., Sander, C. & Vriend, G. Objectively judging the quality of a protein structure from a Ramachandran plot. Comput. Appl. Biosci. 13, 425-430 (1997). (Pubitemid 27384626)
    • (1997) Computer Applications in the Biosciences , vol.13 , Issue.4 , pp. 425-430
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3
  • 2
    • 0038725124 scopus 로고    scopus 로고
    • A use of Ramachandran potentials in protein solution structure determinations
    • DOI 10.1023/A:1024092421649
    • Bertini, I., Cavallaro, G., Luchinat, C. & Poli, I. A use of Ramachandran potentials in protein solution structure determinations. J. Biomol. NMR 26, 355-366 (2003). (Pubitemid 36818135)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.4 , pp. 355-366
    • Bertini, I.1    Cavallaro, G.2    Luchinat, C.3    Poli, I.4
  • 4
    • 34249874640 scopus 로고    scopus 로고
    • Refinement of NMR-determined protein structures with database derived mean-force potentials
    • DOI 10.1002/prot.21358
    • Wu, D., Jernigan, R. & Wu, Z. Refinement of NMR-determined protein structures with database derived mean-force potentials. Proteins 68, 232-242 (2007). (Pubitemid 46871597)
    • (2007) Proteins: Structure, Function and Genetics , vol.68 , Issue.1 , pp. 232-242
    • Wu, D.1    Jernigan, R.2    Wu, Z.3
  • 5
    • 77949333015 scopus 로고    scopus 로고
    • A novel approach to segregate and identify functional loop regions in protein structures using their Ramachandran maps
    • Kumar, M.V. & Swaminathan, R. A novel approach to segregate and identify functional loop regions in protein structures using their Ramachandran maps. Proteins 78, 900-916 (2010).
    • (2010) Proteins , vol.78 , pp. 900-916
    • Kumar, M.V.1    Swaminathan, R.2
  • 9
    • 0032545158 scopus 로고    scopus 로고
    • Stepping through an RNA structure: A novel approach to conformational analysis
    • DOI 10.1006/jmbi.1998.2233
    • Duarte, C.M. & Pyle, A.M. Stepping through an RNA structure: A novel approach to conformational analysis. J. Mol. Biol. 284, 1465-1478 (1998). (Pubitemid 28566081)
    • (1998) Journal of Molecular Biology , vol.284 , Issue.5 , pp. 1465-1478
    • Duarte, C.M.1    Pyle, A.M.2
  • 10
    • 73249135897 scopus 로고    scopus 로고
    • Do conformational biases of simple helical junctions influence RNA folding stability and specificity?
    • Chu, V.B. et al. Do conformational biases of simple helical junctions influence RNA folding stability and specificity? RNA 15, 2195-2205 (2009).
    • (2009) RNA , vol.15 , pp. 2195-2205
    • Chu, V.B.1
  • 11
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • DOI 10.1017/S0033583503003871
    • Koch, M.H., Vachette, P. & Svergun, D.I. Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution. Q. Rev. Biophys. 36, 147-227 (2003). (Pubitemid 37493573)
    • (2003) Quarterly Reviews of Biophysics , vol.36 , Issue.2 , pp. 147-227
    • Koch, M.H.J.1    Vachette, P.2    Svergun, D.I.3
  • 12
    • 0025663739 scopus 로고
    • Internal dynamics of tRNA(Phe) studied by depolarized dynamic light scattering
    • Patkowski, A., Eimer, W. & Dorfmüller, T. Internal dynamics of tRNA(Phe) studied by depolarized dynamic light scattering. Biopolymers 30, 975-983 (1990).
    • (1990) Biopolymers , vol.30 , pp. 975-983
    • Patkowski, A.1    Eimer, W.2    Dorfmüller, T.3
  • 13
    • 44949089510 scopus 로고    scopus 로고
    • Characterization of the dynamics of an essential helix in the U1A protein by time-resolved fluorescence measurements
    • Anunciado, D. et al. Characterization of the dynamics of an essential helix in the U1A protein by time-resolved fluorescence measurements. J. Phys. Chem. B. 112, 6122-6130 (2008).
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 6122-6130
    • Anunciado, D.1
  • 14
    • 62949168954 scopus 로고    scopus 로고
    • Probing complexes with single fluorophores: Factors contributing to dispersion of FRET in DNA/RNA duplexes
    • Cherny, D.I., Eperon, I.C. & Bagshaw, C.R. Probing complexes with single fluorophores: Factors contributing to dispersion of FRET in DNA/RNA duplexes. Eur. Biophys. J. 38, 395-405 (2009).
    • (2009) Eur. Biophys. J. , vol.38 , pp. 395-405
    • Cherny, D.I.1    Eperon, I.C.2    Bagshaw, C.R.3
  • 15
    • 0035010211 scopus 로고    scopus 로고
    • Geometric nomenclature and classification of RNA base pairs
    • DOI 10.1017/S1355838201002515
    • Leontis, N.B. & Westhof, E. Geometric nomenclature and classification of RNA base pairs. RNA 7, 499-512 (2001). (Pubitemid 32416808)
    • (2001) RNA , vol.7 , Issue.4 , pp. 499-512
    • Leontis, N.B.1    Westhof, E.2
  • 16
    • 0025171938 scopus 로고
    • RNA bulges and the helical periodicity of double-stranded RNA
    • DOI 10.1038/343484a0
    • Bhattacharyya, A., Murchie, A. & Lilley, D.M. RNA bulges and the helical periodicity of double-stranded RNA. Nature 343, 484-487 (1990). (Pubitemid 20065240)
    • (1990) Nature , vol.343 , Issue.6257 , pp. 484-487
    • Bhattacharyya, A.1    Murchie, A.I.H.2    Lilley, D.M.J.3
  • 17
    • 0032439514 scopus 로고    scopus 로고
    • Folding of branched RNA species
    • Lilley, D.M. Folding of branched RNA species. Biopolymers 48, 101-112 (1998).
    • (1998) Biopolymers , vol.48 , pp. 101-112
    • Lilley, D.M.1
  • 19
    • 33751248765 scopus 로고    scopus 로고
    • Impact of static and dynamic A-form heterogeneity on the determination of RNA global structural dynamics using NMR residual dipolar couplings
    • DOI 10.1007/s10858-006-9087-9
    • Musselman, C. et al. Impact of static and dynamic A-form heterogeneity on the determination of RNA global structural dynamics using NMR residual dipolar couplings. J. Biomol. NMR 36, 235-249 (2006). (Pubitemid 44782894)
    • (2006) Journal of Biomolecular NMR , vol.36 , Issue.4 , pp. 235-249
    • Musselman, C.1    Pitt, S.W.2    Gulati, K.3    Foster, L.L.4    Andricioaei, I.5    Al-Hashimi, H.M.6
  • 20
    • 0028331914 scopus 로고
    • Interhelix geometry of stems I and II of a self-cleaving hammerhead RNA
    • Gast, F.U., Amiri, K.M. & Hagerman, P.J. Interhelix geometry of stems I and II of a self-cleaving hammerhead RNA. Biochemistry 33, 1788-1796 (1994). (Pubitemid 24089707)
    • (1994) Biochemistry , vol.33 , Issue.7 , pp. 1788-1796
    • Gast, F.-U.1    Amiri, K.M.A.2    Hagerman, P.J.3
  • 21
    • 0029185928 scopus 로고
    • A noncanonical tertiary conformation of a human mitochondrial transfer RNA
    • DOI 10.1021/bi00050a001
    • Leehey, M.A., Squassoni, C.A., Friederich, M.W., Mills, J.B. & Hagerman, P.J. A noncanonical tertiary conformation of a human mitochondrial transfer RNA. Biochemistry 34, 16235-16239 (1995). (Pubitemid 26006464)
    • (1995) Biochemistry , vol.34 , Issue.50 , pp. 16235-16239
    • Leehey, M.A.1    Squassoni, C.A.2    Friederich, M.W.3    Mills, J.B.4    Hagerman, P.J.5
  • 22
    • 0028969693 scopus 로고
    • Bulge-induced bends in RNA: Quantification by transient electric birefringence
    • Zacharias, M. & Hagerman, P.J. Bulge-induced bends in RNA: Quantification by transient electric birefringence. J. Mol. Biol. 247, 486-500 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 486-500
    • Zacharias, M.1    Hagerman, P.J.2
  • 23
    • 0029913806 scopus 로고    scopus 로고
    • The influence of symmetric internal loops on the flexibility of RNA
    • DOI 10.1006/jmbi.1996.0162
    • Zacharias, M. & Hagerman, P.J. The influence of symmetric internal loops on the flexibility of RNA. J. Mol. Biol. 257, 276-289 (1996). (Pubitemid 26114033)
    • (1996) Journal of Molecular Biology , vol.257 , Issue.2 , pp. 276-289
    • Zacharias, M.1    Hagerman, P.J.2
  • 24
    • 0030989905 scopus 로고    scopus 로고
    • Influence of static and dynamic bends on the birefringence decay profile of RNA helices: Brownian dynamics simulations
    • Zacharias, M. & Hagerman, P.J. Influence of static and dynamic bends on the birefringence decay profile of RNA helices: Brownian dynamics simulations. Biophys. J. 73, 318-332 (1997). (Pubitemid 27274129)
    • (1997) Biophysical Journal , vol.73 , Issue.1 , pp. 318-332
    • Zacharias, M.1    Hagerman, P.J.2
  • 25
    • 0029100264 scopus 로고
    • Relative orientation of RNA helices in a group 1 ribozyme determined by helix extension electron microscopy
    • Nakamura, T.M., Wang, Y.H., Zaug, A.J., Griffith, J.D. & Cech, T.R. Relative orientation of RNA helices in a group 1 ribozyme determined by helix extension electron microscopy. EMBO J. 14, 4849 (1995).
    • (1995) EMBO J. , vol.14 , pp. 4849
    • Nakamura, T.M.1    Wang, Y.H.2    Zaug, A.J.3    Griffith, J.D.4    Cech, T.R.5
  • 26
    • 0028004021 scopus 로고
    • Global conformation of a self-cleaving hammerhead RNA
    • DOI 10.1021/bi00249a003
    • Amiri, K.M.A. & Hagerman, P.J. Global conformation of a self-cleaving hammerhead RNA. Biochemistry 33, 13172-13177 (1994). (Pubitemid 24373231)
    • (1994) Biochemistry , vol.33 , Issue.45 , pp. 13172-13177
    • Amiri, K.M.A.1    Hagerman, P.J.2
  • 27
    • 0036290269 scopus 로고    scopus 로고
    • Concerted motions in HIV-1 TAR RNA may allow access to bound state conformations: RNA dynamics from NMR residual dipolar couplings
    • DOI 10.1006/jmbi.2001.5235
    • Al-Hashimi, H.M. et al. Concerted motions in HIV-1 TAR RNA may allow access to bound state conformations: RNA dynamics from NMR residual dipolar couplings. J. Mol. Biol. 315, 95-102 (2002). (Pubitemid 34722113)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.2 , pp. 95-102
    • Al-Hashimi, H.M.1    Gosser, Y.2    Gorin, A.3    Hu, W.4    Majumdar, A.5    Patel, D.J.6
  • 28
    • 31944446215 scopus 로고    scopus 로고
    • Resolving the motional modes that code for RNA adaptation
    • DOI 10.1126/science.1119488
    • Zhang, Q., Sun, X., Watt, E.D. & Al-Hashimi, H.M. Resolving the motional modes that code for RNA adaptation. Science 311, 653-656 (2006). (Pubitemid 43191308)
    • (2006) Science , vol.311 , Issue.5761 , pp. 653-656
    • Zhang, Q.1    Sun, X.2    Watt, E.D.3    Al-Hashimi, H.M.4
  • 29
    • 37549002149 scopus 로고    scopus 로고
    • Dynamics of large elongated RNA by NMR carbon relaxation
    • Hansen, A.L. & Al-Hashimi, H.M. Dynamics of large elongated RNA by NMR carbon relaxation. J. Am. Chem. Soc. 129, 16072-16082 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 16072-16082
    • Hansen, A.L.1    Al-Hashimi, H.M.2
  • 30
    • 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
  • 31
    • 33846443976 scopus 로고    scopus 로고
    • 2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation
    • DOI 10.1261/rna.264207
    • Getz, M.M., Andrews, A.J., Fierke, C.A. & Al-Hashimi, H.M. Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. RNA 13, 251-266 (2007). (Pubitemid 46147900)
    • (2007) RNA , vol.13 , Issue.2 , pp. 251-266
    • Getz, M.M.1    Andrews, A.J.2    Fierke, C.A.3    Al-Hashimi, H.M.4
  • 32
    • 40149085374 scopus 로고    scopus 로고
    • Extending the NMR spatial resolution limit for RNA by motional couplings
    • DOI 10.1038/nmeth.1180, PII NMETH.1180
    • Zhang, Q. & Al-Hashimi, H.M. Extending the NMR spatial resolution limit for RNA by motional couplings. Nat. Methods 5, 243-245 (2008). (Pubitemid 351325648)
    • (2008) Nature Methods , vol.5 , Issue.3 , pp. 243-245
    • Zhang, Q.1    Al-Hashimi, H.M.2
  • 33
    • 67849097846 scopus 로고    scopus 로고
    • Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R(1rho) NMR spectroscopy
    • Hansen, A.L., Nikolova, E.N., Casiano-Negroni, A. & Al-Hashimi, H.M. Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R(1rho) NMR spectroscopy. J. Am. Chem. Soc. 131, 3818-3819 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3818-3819
    • Hansen, A.L.1    Nikolova, E.N.2    Casiano-Negroni, A.3    Al-Hashimi, H.M.4
  • 34
    • 70350091410 scopus 로고    scopus 로고
    • Domain-elongation NMR spectroscopy yields new insights into RNA dynamics and adaptive recognition
    • Zhang, Q. & Al-Hashimi, H.M. Domain-elongation NMR spectroscopy yields new insights into RNA dynamics and adaptive recognition. RNA 15, 1941-1948 (2009).
    • (2009) RNA , vol.15 , pp. 1941-1948
    • Zhang, Q.1    Al-Hashimi, H.M.2
  • 35
    • 72149096007 scopus 로고    scopus 로고
    • Variable helix elongation as a tool to modulate RNA alignment and motional couplings
    • Dethoff, E.A., Hansen, A.L., Zhang, Q. & Al-Hashimi, H.M. Variable helix elongation as a tool to modulate RNA alignment and motional couplings. J. Magn. Reson. 202, 117-121 (2010).
    • (2010) J. Magn. Reson. , vol.202 , pp. 117-121
    • Dethoff, E.A.1    Hansen, A.L.2    Zhang, Q.3    Al-Hashimi, H.M.4
  • 36
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • DOI 10.1016/j.sbi.2005.08.006, PII S0959440X05001545, Carbohydrates and Glycoconjugates/Biophysical Methods
    • Bax, A. & Grishaev, A. Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr. Opin. Struct. Biol. 15, 563-570 (2005). (Pubitemid 41393488)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 38
    • 0036601217 scopus 로고    scopus 로고
    • Residual dipolar couplings in nucleic acid structure determination
    • DOI 10.1016/S0959-440X(02)00328-7
    • MacDonald, D. & Lu, P. Residual dipolar couplings in nucleic acid structure determination. Curr. Opin. Struct. Biol. 12, 337-343 (2002). (Pubitemid 34804615)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.3 , pp. 337-343
    • MacDonald, D.1    Lu, P.2
  • 39
    • 34249898353 scopus 로고    scopus 로고
    • +-induced changes in the HIV-1 TAR conformational dynamics using NMR residual dipolar couplings: New insights into the role of counterions and electrostatic interactions in adaptive recognition
    • DOI 10.1021/bi700335n
    • Casiano-Negroni, A., Sun, X. & Al-Hashimi, H.M. Probing Na(+)-induced changes in the HIV-1 TAR conformational dynamics using NMR residual dipolar couplings: New insights into the role of counterions and electrostatic interactions in adaptive recognition. Biochemistry 46, 6525-6535 (2007). (Pubitemid 46870118)
    • (2007) Biochemistry , vol.46 , Issue.22 , pp. 6525-6535
    • Casiano-Negroni, A.1    Sun, X.2    Al-Hashimi, H.M.3
  • 40
    • 34547820982 scopus 로고    scopus 로고
    • NMR studies of RNA dynamics and structural plasticity using NMR residual diopolar couplings
    • DOI 10.1002/bip.20765
    • Getz, M., Sun, X., Casiano-Negroni, A., Zhang, Q. & Al-Hashimi, H.M. NMR studies of RNA dynamics and structural plasticity using NMR residual dipolar couplings. Biopolymers 86, 384-402 (2007). (Pubitemid 47237806)
    • (2007) Biopolymers , vol.86 , Issue.5-6 , pp. 384-402
    • Getz, M.1    Sun, X.2    Casiano-Negroni, A.3    Zhang, Q.4    Al-Hashimi, H.M.5
  • 41
    • 34250728646 scopus 로고    scopus 로고
    • Characterizing the relative orientation and dynamics of RNA A-form helices using NMR residual dipolar couplings
    • DOI 10.1038/nprot.2007.221, PII NPROT.2007.221
    • Bailor, M.H. et al. Characterizing the relative orientation and dynamics of RNA A-form helices using NMR residual dipolar couplings. Nat. Protoc. 2, 1536-1546 (2007). (Pubitemid 46957313)
    • (2007) Nature Protocols , vol.2 , Issue.6 , pp. 1536-1546
    • Bailor, M.H.1    Musselman, C.2    Hansen, A.L.3    Gulati, K.4    Patel, D.J.5    Al-Hashimi, H.M.6
  • 42
    • 74249115345 scopus 로고    scopus 로고
    • Topology links RNA secondary structure with global conformation, dynamics, and adaptation
    • Bailor, M.H., Sun, X. & Al-Hashimi, H.M. Topology links RNA secondary structure with global conformation, dynamics, and adaptation. Science 327, 202-206 (2010).
    • (2010) Science , vol.327 , pp. 202-206
    • Bailor, M.H.1    Sun, X.2    Al-Hashimi, H.M.3
  • 44
    • 0019764554 scopus 로고
    • DNA and RNA oligomer thermodynamics: The effect of mismatched bases on double-helix stability
    • Nelson, J.W., Martin, F.H. & Tinoco, I. DNA and RNA oligomer thermodynamics: The effect of mismatched bases on double-helix stability. Biopolymers 20, 2509-2531 (1981).
    • (1981) Biopolymers , vol.20 , pp. 2509-2531
    • Nelson, J.W.1    Martin, F.H.2    Tinoco, I.3
  • 45
    • 0021166273 scopus 로고
    • Local mobility of nucleic acids as determined from crystallographic data. I. RNA and B form DNA
    • Holbrook, S.R. & Kim, S.H. Local mobility of nucleic acids as determined from crystallographic data. I. RNA and B form DNA. J. Mol. Biol. 173, 361-388 (1984). (Pubitemid 14128706)
    • (1984) Journal of Molecular Biology , vol.173 , Issue.3 , pp. 361-388
    • Holdbrook, S.R.1    Kim, S.H.2
  • 46
    • 0000335508 scopus 로고    scopus 로고
    • Conformational properties of the deoxyribose and ribose moieties of nucleic acids: A quantum mechanical study
    • Foloppe, N. & MacKerell, A.D. Jr. Conformational properties of the deoxyribose and ribose moieties of nucleic acids: A quantum mechanical study. J. Phys. Chem. B. 102, 6669-6678 (1998). (Pubitemid 128586700)
    • (1998) Journal of Physical Chemistry B , vol.102 , Issue.34 , pp. 6669-6678
    • Foloppe, N.1    MacKerell Jr., A.D.2
  • 47
    • 0029050831 scopus 로고
    • A nomenclature of junctions and branchpoints in nucleic acids
    • Lilley, D.M. et al. A nomenclature of junctions and branchpoints in nucleic acids. Nucleic Acids Res. 23, 3363-3364 (1995).
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3363-3364
    • Lilley, D.M.1
  • 51
    • 66349121080 scopus 로고    scopus 로고
    • Approximate reconstruction of continuous spatially complex domain motions by multialignment NMR residual dipolar couplings
    • Fisher, C.K. & Al-Hashimi, H.M. Approximate reconstruction of continuous spatially complex domain motions by multialignment NMR residual dipolar couplings. J. Phys. Chem. B. 113, 6173-6176 (2009).
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 6173-6176
    • Fisher, C.K.1    Al-Hashimi, H.M.2
  • 53
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi, J.A., Andrec, M., Fischer, M.W.F. & Prestegard, J.H. Order matrix analysis of residual dipolar couplings using singular value decomposition. J. Mag. Reson. 138, 334-342 (1999). (Pubitemid 129608294)
    • (1999) Journal of Magnetic Resonance , vol.138 , Issue.2 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.F.3    Prestegard, J.H.4
  • 54
    • 77955405123 scopus 로고    scopus 로고
    • Assemble: An interactive graphical tool to analyze and build RNA architectures at the 2D and 3D levels
    • Jossinet, F., Ludwig, T.E. & Westhof, E. Assemble: An interactive graphical tool to analyze and build RNA architectures at the 2D and 3D levels. Bioinformatics 26, 2057-2059 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 2057-2059
    • Jossinet, F.1    Ludwig, T.E.2    Westhof, E.3
  • 55
    • 0024556774 scopus 로고
    • Conformational and helicoidal analysis of 30 PS of molecular dynamics on the d(CGCGAATTCGCG) double helix: 'Curves, dials and windows
    • Ravishanker, G., Swaminathan, S., Beveridge, D.L., Lavery, R. & Sklenar, H. Conformational and helicoidal analysis of 30 PS of molecular dynamics on the d (CGCGAATTCGCG) double helix: 'curves', dials and windows. J. Biomol. Struct. Dyn. 6, 669-699 (1989). (Pubitemid 19079753)
    • (1989) Journal of Biomolecular Structure and Dynamics , vol.6 , Issue.4 , pp. 669-699
    • Ravishanker, G.1    Swaminathan, S.2    Beveridge, D.L.3    Lavery, R.4    Sklenar, H.5
  • 56
    • 0032522139 scopus 로고    scopus 로고
    • DNA bending: The prevalence of kinkiness and the virtues of normality
    • DOI 10.1093/nar/26.8.1906
    • Dickerson, R.E. DNA bending: The prevalence of kinkiness and the virtues of normality. Nucleic Acids Res. 26, 1906-1926 (1998). (Pubitemid 28291723)
    • (1998) Nucleic Acids Research , vol.26 , Issue.8 , pp. 1906-1926
    • Dickerson, R.E.1
  • 57
    • 0242396923 scopus 로고    scopus 로고
    • 3DNA: A software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures
    • DOI 10.1093/nar/gkg680
    • Lu, X.J. & Olson, W.K. 3DNA: A software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures. Nucleic Acids Res. 31, 5108-5121 (2003). (Pubitemid 37441878)
    • (2003) Nucleic Acids Research , vol.31 , Issue.17 , pp. 5108-5121
    • Lu, X.-J.1    Olson, W.K.2
  • 58
    • 0031592942 scopus 로고    scopus 로고
    • Structure and conformation of helical nucleic acids: Analysis program (SCHNAaP)
    • DOI 10.1006/jmbi.1997.1346
    • Lu, X.J., El Hassan, M.A. & Hunter, C.A. Structure and conformation of helical nucleic acids: Analysis program (SCHNAaP). J. Mol. Biol. 273, 668-680 (1997). (Pubitemid 27488808)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.3 , pp. 668-680
    • Lu, X.-J.1    El Hassan, M.A.2    Hunter, C.A.3
  • 59
    • 0029023343 scopus 로고
    • NUPARM and NUCGEN: Software for analysis and generation of sequence dependent nucleic acid structures
    • Bansal, M., Bhattacharyya, D. & Ravi, B. NUPARM and NUCGEN: Software for analysis and generation of sequence dependent nucleic acid structures. Comput. Appl. Biosci. 11, 281-287 (1995).
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 281-287
    • Bansal, M.1    Bhattacharyya, D.2    Ravi, B.3
  • 60
    • 0036890275 scopus 로고    scopus 로고
    • Consistent treatment of inter- and intramolecular polarization in molecular mechanics calculations
    • DOI 10.1002/jcc.10127
    • Ren, P. & Ponder, J.W. Consistent treatment of inter- and intramolecular polarization in molecular mechanics calculations. J. Comput. Chem. 23, 1497-1506 (2002). (Pubitemid 35330852)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.16 , pp. 1497-1506
    • Ren, P.1    Ponder, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.