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Volumn 1850, Issue 5, 2015, Pages 1091-1098

Coupled binding-bending-folding: The complex conformational dynamics of protein-DNA binding studied by atomistic molecular dynamics simulations

Author keywords

DNA bending; Molecular dynamics; Protein folding; Protein DNA; Simulation

Indexed keywords

BINDING PROTEIN; DNA; DNA BINDING PROTEIN; PROTEIN BINDING;

EID: 84923182763     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.08.009     Document Type: Review
Times cited : (29)

References (182)
  • 1
    • 0037472782 scopus 로고    scopus 로고
    • Modulation of DNA-binding domains for sequence-specific DNA recognition
    • R. Marmorstein, and M.X. Fitzgerald Modulation of DNA-binding domains for sequence-specific DNA recognition Gene 304 2003 1 12
    • (2003) Gene , vol.304 , pp. 1-12
    • Marmorstein, R.1    Fitzgerald, M.X.2
  • 2
    • 0030736323 scopus 로고    scopus 로고
    • Protein-DNA recognition complexes: Conservation of structure and binding energy in the transition state
    • L. Jen-Jacobson Protein-DNA recognition complexes: conservation of structure and binding energy in the transition state Biopolymers 44 1997 153 180
    • (1997) Biopolymers , vol.44 , pp. 153-180
    • Jen-Jacobson, L.1
  • 3
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic-acids.1. Models and theory
    • O.G. Berg, R.B. Winter, and P.H. Vonhippel Diffusion-driven mechanisms of protein translocation on nucleic-acids.1. Models and theory Biochemistry 20 1981 6929 6948
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Vonhippel, P.H.3
  • 5
    • 49449107340 scopus 로고    scopus 로고
    • Visualizing one-dimensional diffusion of proteins along DNA
    • J. Gorman, and E.C. Greene Visualizing one-dimensional diffusion of proteins along DNA Nat. Struct. Mol. Biol. 15 2008 768 774
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 768-774
    • Gorman, J.1    Greene, E.C.2
  • 6
    • 0032986554 scopus 로고    scopus 로고
    • One-dimensional diffusion of proteins along DNA - Its biological and chemical significance revealed by single-molecule measurements
    • N. Shimamoto One-dimensional diffusion of proteins along DNA - Its biological and chemical significance revealed by single-molecule measurements J. Biol. Chem. 274 1999 15293 15296
    • (1999) J. Biol. Chem. , vol.274 , pp. 15293-15296
    • Shimamoto, N.1
  • 7
    • 34249932435 scopus 로고    scopus 로고
    • Probing transcription factor dynamics at the single-molecule level in a living cell
    • J. Elf, G.-W. Li, and X.S. Xie Probing transcription factor dynamics at the single-molecule level in a living cell Science 316 2007 1191 1194
    • (2007) Science , vol.316 , pp. 1191-1194
    • Elf, J.1    Li, G.-W.2    Xie, X.S.3
  • 9
    • 0034435652 scopus 로고    scopus 로고
    • Structural and thermodynamic strategies for site-specific DNA binding proteins
    • L. Jen-Jacobson, L.E. Engler, and L.A. Jacobson Structural and thermodynamic strategies for site-specific DNA binding proteins Structure 8 2000 1015 1023
    • (2000) Structure , vol.8 , pp. 1015-1023
    • Jen-Jacobson, L.1    Engler, L.E.2    Jacobson, L.A.3
  • 10
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • R.S. Spolar, and M.T. Record Coupling of local folding to site-specific binding of proteins to DNA Science 263 1994 777 784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 12
    • 0037372298 scopus 로고    scopus 로고
    • Protein folding coupled to DNA binding in the catalytic domain of bacteriophage lambda integrase detected by mass spectrometry
    • H.B. Kamadurai, S. Subramaniam, R.B. Jones, K.B. Green-Church, and M.P. Foster Protein folding coupled to DNA binding in the catalytic domain of bacteriophage lambda integrase detected by mass spectrometry Protein Sci. 12 2003 620 626
    • (2003) Protein Sci. , vol.12 , pp. 620-626
    • Kamadurai, H.B.1    Subramaniam, S.2    Jones, R.B.3    Green-Church, K.B.4    Foster, M.P.5
  • 13
    • 3042855283 scopus 로고    scopus 로고
    • The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA
    • J.J. Love, X. Li, J. Chung, H.J. Dyson, and P.E. Wright The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA Biochemistry 43 2004 8725 8734
    • (2004) Biochemistry , vol.43 , pp. 8725-8734
    • Love, J.J.1    Li, X.2    Chung, J.3    Dyson, H.J.4    Wright, P.E.5
  • 15
    • 0033591443 scopus 로고    scopus 로고
    • Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding
    • J.F. Chang, K. Phillips, T. Lundback, M. Gstaiger, J.E. Ladbury, and B. Luisi Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding J. Mol. Biol. 288 1999 941 952
    • (1999) J. Mol. Biol. , vol.288 , pp. 941-952
    • Chang, J.F.1    Phillips, K.2    Lundback, T.3    Gstaiger, M.4    Ladbury, J.E.5    Luisi, B.6
  • 16
    • 0032489433 scopus 로고    scopus 로고
    • DNA-mediated folding and assembly of MyoD-E47 heterodimers
    • H. Wendt, R.M. Thomas, and T. Ellenberger DNA-mediated folding and assembly of MyoD-E47 heterodimers J. Biol. Chem. 273 1998 5735 5743
    • (1998) J. Biol. Chem. , vol.273 , pp. 5735-5743
    • Wendt, H.1    Thomas, R.M.2    Ellenberger, T.3
  • 19
    • 0031238604 scopus 로고    scopus 로고
    • DNA recognition and bending
    • R.K. Allemann, and M. Egli DNA recognition and bending Chem. Biol. 4 1997 643 650
    • (1997) Chem. Biol. , vol.4 , pp. 643-650
    • Allemann, R.K.1    Egli, M.2
  • 20
    • 57749209893 scopus 로고    scopus 로고
    • The major architects of chromatin: Architectural proteins in bacteria, archaea and eukaryotes
    • M.S. Luijsterburg, M.F. White, R. van Driel, and R.T. Dame The major architects of chromatin: architectural proteins in bacteria, archaea and eukaryotes Crit. Rev. Biochem. Mol. Biol. 43 2008 393 418
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 393-418
    • Luijsterburg, M.S.1    White, M.F.2    Van Driel, R.3    Dame, R.T.4
  • 22
    • 80054758750 scopus 로고    scopus 로고
    • Surviving the sun: Repair and bypass of DNA UV lesions
    • W. Yang Surviving the sun: repair and bypass of DNA UV lesions Protein Sci. 20 2011 1781 1789
    • (2011) Protein Sci. , vol.20 , pp. 1781-1789
    • Yang, W.1
  • 23
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • M. Karplus, and J.A. McCammon Molecular dynamics simulations of biomolecules Nat. Struct. Biol. 9 2002 646 652
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 24
    • 41949124146 scopus 로고    scopus 로고
    • Molecular dynamics simulations of nucleic acid-protein complexes
    • A.D. Mackerell, and L. Nilsson Molecular dynamics simulations of nucleic acid-protein complexes Curr. Opin. Struct. Biol. 18 2008 194 199
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 194-199
    • Mackerell, A.D.1    Nilsson, L.2
  • 26
    • 33748253737 scopus 로고    scopus 로고
    • Simulation of conformational transitions
    • A. van der Vaart Simulation of conformational transitions Theor. Chem. Acc. 116 2006 183 193
    • (2006) Theor. Chem. Acc. , vol.116 , pp. 183-193
    • Van Der Vaart, A.1
  • 27
    • 80855148257 scopus 로고    scopus 로고
    • Development and application of enhanced sampling techniques to simulate the long-time scale dynamics of biomolecular systems
    • J. Spiriti, H. Kamberaj, and A. Van Der Vaart Development and application of enhanced sampling techniques to simulate the long-time scale dynamics of biomolecular systems Int. J. Quantum Chem. 112 2012 33 43
    • (2012) Int. J. Quantum Chem. , vol.112 , pp. 33-43
    • Spiriti, J.1    Kamberaj, H.2    Van Der Vaart, A.3
  • 28
    • 84860477162 scopus 로고    scopus 로고
    • Frontiers in molecular dynamics simulations of DNA
    • A. Perez, F. Javier Luque, and M. Orozco Frontiers in molecular dynamics simulations of DNA Acc. Chem. Res. 45 2012 196 205
    • (2012) Acc. Chem. Res. , vol.45 , pp. 196-205
    • Perez, A.1    Javier Luque, F.2    Orozco, M.3
  • 29
    • 84855661433 scopus 로고    scopus 로고
    • Optimization of the CHARMM additive force field for DNA: Improved treatment of the BI/BII conformational equilibrium
    • K. Hart, N. Foloppe, C.M. Baker, E.J. Denning, L. Nilsson, and A.D. MacKerell Optimization of the CHARMM additive force field for DNA: improved treatment of the BI/BII conformational equilibrium J. Chem. Theory Comput. 8 2012 348 362
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 348-362
    • Hart, K.1    Foloppe, N.2    Baker, C.M.3    Denning, E.J.4    Nilsson, L.5    MacKerell, A.D.6
  • 30
    • 34250318638 scopus 로고    scopus 로고
    • Refinement of the AMBER force field for nucleic acids: Improving the description of α/γ conformers
    • A. Perez, I. Marchan, D. Svozil, J. Sponer, T.E. Cheatham III, C.A. Laughton, and M. Orozco Refinement of the AMBER force field for nucleic acids: improving the description of α/γ conformers Biophys. J. 92 2007 3817 3829
    • (2007) Biophys. J. , vol.92 , pp. 3817-3829
    • Perez, A.1    Marchan, I.2    Svozil, D.3    Sponer, J.4    Cheatham, T.E.5    Laughton, C.A.6    Orozco, M.7
  • 32
    • 49449085241 scopus 로고    scopus 로고
    • Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations
    • I.S. Joung, and T.E. Cheatham III Determination of alkali and halide monovalent ion parameters for use in explicitly solvated biomolecular simulations J. Phys. Chem. B 112 2008 9020 9041
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9020-9041
    • Joung, I.S.1    Cheatham, T.E.2
  • 33
    • 80052820313 scopus 로고    scopus 로고
    • Refinement of the Cornell et al. Nucleic acids force field based on reference quantum chemical calculations of glycosidic torsion profiles
    • M. Zgarbova, M. Otyepka, J. Sponer, A. Mladek, P. Banas, T.E. Cheatham III, and P. Jurecka Refinement of the Cornell et al. Nucleic acids force field based on reference quantum chemical calculations of glycosidic torsion profiles J. Chem. Theory Comput. 7 2011 2886 2902
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 2886-2902
    • Zgarbova, M.1    Otyepka, M.2    Sponer, J.3    Mladek, A.4    Banas, P.5    Cheatham, T.E.6    Jurecka, P.7
  • 35
    • 0020262664 scopus 로고
    • Computer simulation of DNA double-helix dynamics
    • M. Levitt Computer simulation of DNA double-helix dynamics Cold Spring Harb. Symp. Quant. Biol. 47 1983 251 262
    • (1983) Cold Spring Harb. Symp. Quant. Biol. , vol.47 , pp. 251-262
    • Levitt, M.1
  • 36
    • 0001555216 scopus 로고
    • A molecular-dynamics simulation of double-helical B-DNA including counterions and water
    • G.L. Seibel, U.C. Singh, and P.A. Kollman A molecular-dynamics simulation of double-helical B-DNA including counterions and water Proc. Natl. Acad. Sci. U. S. A. 82 1985 6537 6540
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 6537-6540
    • Seibel, G.L.1    Singh, U.C.2    Kollman, P.A.3
  • 38
    • 0032459726 scopus 로고    scopus 로고
    • Molecular dynamic simulations of environment and sequence dependent DNA conformations: The development of the BMS nucleic acid force field and comparison with experimental results
    • D.R. Langley Molecular dynamic simulations of environment and sequence dependent DNA conformations: The development of the BMS nucleic acid force field and comparison with experimental results J. Biomol. Struct. Dyn. 16 1998 487 509
    • (1998) J. Biomol. Struct. Dyn. , vol.16 , pp. 487-509
    • Langley, D.R.1
  • 39
    • 0035974484 scopus 로고    scopus 로고
    • Molecular mechanical models for organic and biological systems going beyond the atom centered two body additive approximation: Aqueous solution free energies of methanol and N-methyl acetamide, nucleic acid base, and amide hydrogen bonding and chloroform/water partition coefficients of the nucleic acid bases
    • P. Cieplak, J. Caldwell, and P. Kollman Molecular mechanical models for organic and biological systems going beyond the atom centered two body additive approximation: aqueous solution free energies of methanol and N-methyl acetamide, nucleic acid base, and amide hydrogen bonding and chloroform/water partition coefficients of the nucleic acid bases J. Comput. Chem. 22 2001 1048 1057
    • (2001) J. Comput. Chem. , vol.22 , pp. 1048-1057
    • Cieplak, P.1    Caldwell, J.2    Kollman, P.3
  • 40
    • 33750904923 scopus 로고    scopus 로고
    • Molecular dynamics simulations of polarizable DNA in crystal environment
    • V. Babin, J. Baucom, T.A. Darden, and C. Sagui Molecular dynamics simulations of polarizable DNA in crystal environment Int. J. Quantum Chem. 106 2006 3260 3269
    • (2006) Int. J. Quantum Chem. , vol.106 , pp. 3260-3269
    • Babin, V.1    Baucom, J.2    Darden, T.A.3    Sagui, C.4
  • 41
    • 33745727284 scopus 로고    scopus 로고
    • Molecular dynamics simulations of DNA with polarizable force fields: Convergence of an ideal B-DNA structure to the crystallographic structure
    • V. Babin, J. Baucom, T.A. Darden, and C. Sagui Molecular dynamics simulations of DNA with polarizable force fields: Convergence of an ideal B-DNA structure to the crystallographic structure J. Phys. Chem. B 110 2006 11571 11581
    • (2006) J. Phys. Chem. B , vol.110 , pp. 11571-11581
    • Babin, V.1    Baucom, J.2    Darden, T.A.3    Sagui, C.4
  • 42
    • 7544244858 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the d(CCAACGTTGG)(2) decamer in crystal environment: Comparison of atomic point-charge, extra-point, and polarizable force fields
    • J. Baucom, T. Transue, M. Fuentes-Cabrera, J.M. Krahn, T.A. Darden, and C. Sagui Molecular dynamics simulations of the d(CCAACGTTGG)(2) decamer in crystal environment: Comparison of atomic point-charge, extra-point, and polarizable force fields J. Chem. Phys. 121 2004 6998 7008
    • (2004) J. Chem. Phys. , vol.121 , pp. 6998-7008
    • Baucom, J.1    Transue, T.2    Fuentes-Cabrera, M.3    Krahn, J.M.4    Darden, T.A.5    Sagui, C.6
  • 45
    • 77953584337 scopus 로고    scopus 로고
    • Polarizable atomic multipole X-ray refinement: Hydration geometry and application to macromolecules
    • T.D. Fenn, M.J. Schnieders, A.T. Brunger, and V.S. Pande Polarizable atomic multipole X-ray refinement: hydration geometry and application to macromolecules Biophys. J. 98 2010 2984 2992
    • (2010) Biophys. J. , vol.98 , pp. 2984-2992
    • Fenn, T.D.1    Schnieders, M.J.2    Brunger, A.T.3    Pande, V.S.4
  • 46
    • 79953902483 scopus 로고    scopus 로고
    • Reintroducing electrostatics into macromolecular crystallographic refinement: Application to neutron crystallography and DNA hydration
    • T.D. Fenn, M.J. Schnieders, M. Mustyakimov, C. Wu, P. Langan, V.S. Pande, and A.T. Brunger Reintroducing electrostatics into macromolecular crystallographic refinement: application to neutron crystallography and DNA hydration Structure 19 2011 523 533
    • (2011) Structure , vol.19 , pp. 523-533
    • Fenn, T.D.1    Schnieders, M.J.2    Mustyakimov, M.3    Wu, C.4    Langan, P.5    Pande, V.S.6    Brunger, A.T.7
  • 48
    • 84900474707 scopus 로고    scopus 로고
    • All-atom polarizable force field for DNA based on the classical Drude oscillator model
    • A. Savelyev, and A.D. MacKerell Jr. All-atom polarizable force field for DNA based on the classical Drude oscillator model J. Comput. Chem. 35 2014 1219 1239
    • (2014) J. Comput. Chem. , vol.35 , pp. 1219-1239
    • Savelyev, A.1    MacKerell, A.D.2
  • 50
    • 84881405929 scopus 로고    scopus 로고
    • A polarizable force field of dipalmitoylphosphatidylcholine based on the classical Drude model for molecular dynamics simulations of lipids
    • J. Chowdhary, E. Harder, P.E.M. Lopes, L. Huang, A.D. MacKerell Jr., and B. Roux A polarizable force field of dipalmitoylphosphatidylcholine based on the classical Drude model for molecular dynamics simulations of lipids J. Phys. Chem. B 117 2013 9142 9160
    • (2013) J. Phys. Chem. B , vol.117 , pp. 9142-9160
    • Chowdhary, J.1    Harder, E.2    Lopes, P.E.M.3    Huang, L.4    MacKerell, A.D.5    Roux, B.6
  • 51
    • 84881159900 scopus 로고    scopus 로고
    • Polarizable empirical force field for acyclic polyalcohols based on the classical Drude oscillator
    • X. He, P.E.M. Lopes, and A.D. MacKerell Jr. Polarizable empirical force field for acyclic polyalcohols based on the classical Drude oscillator Biopolymers 99 2013 724 738
    • (2013) Biopolymers , vol.99 , pp. 724-738
    • He, X.1    Lopes, P.E.M.2    MacKerell, A.D.3
  • 52
    • 84902951608 scopus 로고    scopus 로고
    • Balancing the interactions of ions, water, and DNA in the Drude polarizable force field
    • A. Savelyev, and A.D. Mackerell Balancing the interactions of ions, water, and DNA in the Drude polarizable force field J. Phys. Chem. B 118 2014 6742 6757
    • (2014) J. Phys. Chem. B , vol.118 , pp. 6742-6757
    • Savelyev, A.1    Mackerell, A.D.2
  • 53
    • 84982060514 scopus 로고
    • Röntgenuntersuchung gelöster Fadenmoleküle
    • O. Kratky, and G. Porod Röntgenuntersuchung gelöster Fadenmoleküle Recl. Trav. Chim. Pays-Bas 68 1949 1106 1123
    • (1949) Recl. Trav. Chim. Pays-Bas , vol.68 , pp. 1106-1123
    • Kratky, O.1    Porod, G.2
  • 54
    • 77957240284 scopus 로고    scopus 로고
    • DNA curvature and flexibility in vitro and in vivo
    • J.P. Peters, and L.J. Maher DNA curvature and flexibility in vitro and in vivo Q. Rev. Biophys. 44 2010 23 63
    • (2010) Q. Rev. Biophys. , vol.44 , pp. 23-63
    • Peters, J.P.1    Maher, L.J.2
  • 58
    • 33646158918 scopus 로고    scopus 로고
    • The contribution of transient counterion imbalances to DNA bending fluctuations
    • G.S. Manning The contribution of transient counterion imbalances to DNA bending fluctuations Biophys. J. 90 2006 3208 3215
    • (2006) Biophys. J. , vol.90 , pp. 3208-3215
    • Manning, G.S.1
  • 59
    • 84862168795 scopus 로고    scopus 로고
    • Adaptive umbrella sampling on roll angles indicates that DNA bending through large angles is aided by ionic screening
    • J. Spiriti, H. Kamberaj, A. De Graff, M.F. Thorpe, and A. van der Vaart Adaptive umbrella sampling on roll angles indicates that DNA bending through large angles is aided by ionic screening J. Chem. Theory Comput. 8 2012 2145 2156
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 2145-2156
    • Spiriti, J.1    Kamberaj, H.2    De Graff, A.3    Thorpe, M.F.4    Van Der Vaart, A.5
  • 60
    • 84856748887 scopus 로고    scopus 로고
    • Do monovalent mobile ions affect DNA's flexibility at high salt content?
    • A. Savelyev Do monovalent mobile ions affect DNA's flexibility at high salt content? Phys. Chem. Chem. Phys. 14 2012 2250 2254
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 2250-2254
    • Savelyev, A.1
  • 63
    • 0036569686 scopus 로고    scopus 로고
    • Bending of DNA by asymmetric charge neutralization: All-atom energy simulations
    • K.M. Kosikov, A.A. Gorin, X.J. Lu, W.K. Olson, and G.S. Manning Bending of DNA by asymmetric charge neutralization: all-atom energy simulations J. Am. Chem. Soc. 124 2002 4838 4847
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4838-4847
    • Kosikov, K.M.1    Gorin, A.A.2    Lu, X.J.3    Olson, W.K.4    Manning, G.S.5
  • 65
    • 33751233867 scopus 로고    scopus 로고
    • The persistence length of DNA is reached from the persistence length of its null isomer through an internal electrostatic stretching force
    • G.S. Manning The persistence length of DNA is reached from the persistence length of its null isomer through an internal electrostatic stretching force Biophys. J. 91 2006 3607 3616
    • (2006) Biophys. J. , vol.91 , pp. 3607-3616
    • Manning, G.S.1
  • 66
    • 82555175927 scopus 로고    scopus 로고
    • Is DNA's rigidity dominated by electrostatic or nonelectrostatic interactions?
    • A. Savelyev, C.K. Materese, and G.A. Papoian Is DNA's rigidity dominated by electrostatic or nonelectrostatic interactions? J. Am. Chem. Soc. 133 2011 19290 19293
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19290-19293
    • Savelyev, A.1    Materese, C.K.2    Papoian, G.A.3
  • 68
    • 0025355712 scopus 로고
    • Application of the method of phage-T4 DNA ligase-catalyzed ring closure to the study of DNA structure. 2. NaCl dependence of DNA flexibility and helical repeat
    • W.H. Taylor, and P.J. Hagerman Application of the method of phage-T4 DNA ligase-catalyzed ring closure to the study of DNA structure. 2. NaCl dependence of DNA flexibility and helical repeat J. Mol. Biol. 212 1990 363 376
    • (1990) J. Mol. Biol. , vol.212 , pp. 363-376
    • Taylor, W.H.1    Hagerman, P.J.2
  • 70
    • 85015087906 scopus 로고    scopus 로고
    • Ten years of tension: Single-molecule DNA mechanics
    • C. Bustamante, Z. Bryant, and S. Smith Ten years of tension: single-molecule DNA mechanics Nature 421 2003 423 427
    • (2003) Nature , vol.421 , pp. 423-427
    • Bustamante, C.1    Bryant, Z.2    Smith, S.3
  • 71
    • 84985648233 scopus 로고
    • Microscopic persistence length of native DNA - Its relation to average molecular dimensions
    • A. Bettini, M.R. Pozzan, E. Valdevit, and C. Frontali Microscopic persistence length of native DNA - Its relation to average molecular dimensions Biopolymers 19 1980 1689 1694
    • (1980) Biopolymers , vol.19 , pp. 1689-1694
    • Bettini, A.1    Pozzan, M.R.2    Valdevit, E.3    Frontali, C.4
  • 72
    • 77951977112 scopus 로고    scopus 로고
    • The relationship between curvature, flexibility and persistence length in the tropomyosin coiled-coil
    • X. Li, W. Lehman, and S. Fischer The relationship between curvature, flexibility and persistence length in the tropomyosin coiled-coil J. Struct. Biol. 170 2010 313 318
    • (2010) J. Struct. Biol. , vol.170 , pp. 313-318
    • Li, X.1    Lehman, W.2    Fischer, S.3
  • 73
    • 33845381916 scopus 로고    scopus 로고
    • Evaluation of elastic properties of atomistic DNA models
    • A.K. Mazur Evaluation of elastic properties of atomistic DNA models Biophys. J. 91 2006 4507 4518
    • (2006) Biophys. J. , vol.91 , pp. 4507-4518
    • Mazur, A.K.1
  • 75
    • 85014002810 scopus 로고    scopus 로고
    • Modeling DNA structure, elasticity, and deformations at the base-pair level
    • B. Mergell, M.R. Ejtehadi, and R. Everaers Modeling DNA structure, elasticity, and deformations at the base-pair level Phys. Rev. E. 68 2003
    • (2003) Phys. Rev. E. , vol.68
    • Mergell, B.1    Ejtehadi, M.R.2    Everaers, R.3
  • 76
    • 49649112706 scopus 로고    scopus 로고
    • Multiscale modeling of nucleic acids: Insights into DNA flexibility
    • Y.J. Bomble, and D.A. Case Multiscale modeling of nucleic acids: insights into DNA flexibility Biopolymers 89 2008 722 731
    • (2008) Biopolymers , vol.89 , pp. 722-731
    • Bomble, Y.J.1    Case, D.A.2
  • 78
    • 2342518189 scopus 로고    scopus 로고
    • Spontaneous sharp bending of double-stranded DNA
    • T.E. Cloutier, and J. Widom Spontaneous sharp bending of double-stranded DNA Mol. Cell 14 2004 355 362
    • (2004) Mol. Cell , vol.14 , pp. 355-362
    • Cloutier, T.E.1    Widom, J.2
  • 79
    • 84865546608 scopus 로고    scopus 로고
    • Extreme bendability of DNA less than 100 base pairs long revealed by single-molecule cyclization
    • R. Vafabakhsh, and T. Ha Extreme bendability of DNA less than 100 base pairs long revealed by single-molecule cyclization Science 337 2012 1097 1101
    • (2012) Science , vol.337 , pp. 1097-1101
    • Vafabakhsh, R.1    Ha, T.2
  • 85
    • 0036293430 scopus 로고    scopus 로고
    • Contribution of the intrinsic curvature to measured DNA persistence length
    • M. Vologodskaia, and A. Vologodskii Contribution of the intrinsic curvature to measured DNA persistence length J. Mol. Biol. 317 2002 205 213
    • (2002) J. Mol. Biol. , vol.317 , pp. 205-213
    • Vologodskaia, M.1    Vologodskii, A.2
  • 86
    • 70349602563 scopus 로고    scopus 로고
    • Probing the conformational distributions of subpersistence length DNA
    • A.J. Mastroianni, D.A. Sivak, P.L. Geisser, and A.P. Alivisatos Probing the conformational distributions of subpersistence length DNA Biophys. J. 97 2009 1408 1417
    • (2009) Biophys. J. , vol.97 , pp. 1408-1417
    • Mastroianni, A.J.1    Sivak, D.A.2    Geisser, P.L.3    Alivisatos, A.P.4
  • 88
    • 33749259954 scopus 로고    scopus 로고
    • Kinking occurs during molecular dynamics simulation of small DNA minicircles
    • F. Lankas, R. Lavery, and J.H. Maddocks Kinking occurs during molecular dynamics simulation of small DNA minicircles Structure 14 2006 1527 1534
    • (2006) Structure , vol.14 , pp. 1527-1534
    • Lankas, F.1    Lavery, R.2    Maddocks, J.H.3
  • 89
    • 79956013643 scopus 로고    scopus 로고
    • Atomistic simulations reveal bubbles, kinks and wrinkles in supercoiled DNA
    • J.S. Mitchell, C.A. Laughton, and S.A. Harris Atomistic simulations reveal bubbles, kinks and wrinkles in supercoiled DNA Nucleic Acids Res. 39 2011 3928 3938
    • (2011) Nucleic Acids Res. , vol.39 , pp. 3928-3938
    • Mitchell, J.S.1    Laughton, C.A.2    Harris, S.A.3
  • 90
    • 0016850069 scopus 로고
    • Kinky helix
    • F.H.C. Crick, and A. Klug Kinky helix Nature 255 1975 530 533
    • (1975) Nature , vol.255 , pp. 530-533
    • Crick, F.H.C.1    Klug, A.2
  • 91
    • 19544379865 scopus 로고    scopus 로고
    • Localized single-stranded bubble mechanism for cyclization of short double helix DNA
    • J. Yan, and J.F. Marko Localized single-stranded bubble mechanism for cyclization of short double helix DNA Phys. Rev. Lett. 93 2004 108108
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 108108
    • Yan, J.1    Marko, J.F.2
  • 93
    • 67649883207 scopus 로고    scopus 로고
    • Local and global effects of strong DNA bending induced during molecular dynamics simulations
    • J. Curuksu, M. Zacharias, R. Lavery, and K. Zakrzewska Local and global effects of strong DNA bending induced during molecular dynamics simulations Nucleic Acids Res. 37 2009 3766 3773
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3766-3773
    • Curuksu, J.1    Zacharias, M.2    Lavery, R.3    Zakrzewska, K.4
  • 94
    • 84867636708 scopus 로고    scopus 로고
    • DNA bending through roll angles is independent of adjacent base pairs
    • J. Spiriti, and A. van der Vaart DNA bending through roll angles is independent of adjacent base pairs J. Phys. Chem. Lett. 3 2012 3029 3033
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 3029-3033
    • Spiriti, J.1    Van Der Vaart, A.2
  • 95
    • 33644791019 scopus 로고    scopus 로고
    • Generalized theory of semiflexible polymers
    • P.A. Wiggins, and P.C. Nelson Generalized theory of semiflexible polymers Phys. Rev. E. 73 2006 31906
    • (2006) Phys. Rev. E. , vol.73 , pp. 31906
    • Wiggins, P.A.1    Nelson, P.C.2
  • 96
    • 84878067644 scopus 로고    scopus 로고
    • DNA bending propensity in the presence of base mismatches: Implications for DNA repair
    • M. Sharma, A.V. Predeus, S. Mukherjee, and M. Feig DNA bending propensity in the presence of base mismatches: implications for DNA repair J. Phys. Chem. B 117 2013 6194 6205
    • (2013) J. Phys. Chem. B , vol.117 , pp. 6194-6205
    • Sharma, M.1    Predeus, A.V.2    Mukherjee, S.3    Feig, M.4
  • 97
    • 42449117606 scopus 로고    scopus 로고
    • Magnitude and direction of DNA bending induced by screw-axis orientation: Influence of sequence mismatches and abasic sites
    • J. Curuksu, K. Zakrzewska, and M. Zacharias Magnitude and direction of DNA bending induced by screw-axis orientation: influence of sequence mismatches and abasic sites Nucleic Acids Res. 36 2008 2268 2283
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2268-2283
    • Curuksu, J.1    Zakrzewska, K.2    Zacharias, M.3
  • 98
    • 84885133326 scopus 로고    scopus 로고
    • Effect of 8-oxoguanine on DNA structure and deformability
    • T. Drsata, M. Kara, M. Zacharias, and F. Lankas Effect of 8-oxoguanine on DNA structure and deformability J. Phys. Chem. B 117 2013 11617 11622
    • (2013) J. Phys. Chem. B , vol.117 , pp. 11617-11622
    • Drsata, T.1    Kara, M.2    Zacharias, M.3    Lankas, F.4
  • 99
    • 84874866920 scopus 로고    scopus 로고
    • Influence of 8-oxoguanosine on the fine structure of DNA studied with biasing-potential replica exchange simulations
    • M. Kara, and M. Zacharias Influence of 8-oxoguanosine on the fine structure of DNA studied with biasing-potential replica exchange simulations Biophys. J. 104 2013 1089 1097
    • (2013) Biophys. J. , vol.104 , pp. 1089-1097
    • Kara, M.1    Zacharias, M.2
  • 100
    • 69249125806 scopus 로고    scopus 로고
    • DNA methylation-mediated epigenetic control
    • A. Rottach, H. Leonhardt, and F. Spada DNA methylation-mediated epigenetic control J. Cell. Biochem. 108 2009 43 51
    • (2009) J. Cell. Biochem. , vol.108 , pp. 43-51
    • Rottach, A.1    Leonhardt, H.2    Spada, F.3
  • 101
    • 22844457491 scopus 로고    scopus 로고
    • DNA methylation and human disease
    • K.D. Robertson DNA methylation and human disease Nat. Rev. Genet. 6 2005 597 610
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 597-610
    • Robertson, K.D.1
  • 102
    • 0037068378 scopus 로고    scopus 로고
    • DNA methylation and cancer
    • P.A. Jones DNA methylation and cancer Oncogene 21 2002 5358 5360
    • (2002) Oncogene , vol.21 , pp. 5358-5360
    • Jones, P.A.1
  • 106
    • 84888223867 scopus 로고    scopus 로고
    • Understanding the connection between epigenetic DNA methylation and nucleosome positioning from computer simulations
    • G. Portella, F. Battistini, and M. Orozco Understanding the connection between epigenetic DNA methylation and nucleosome positioning from computer simulations PLoS Comput. Biol. 9 2013
    • (2013) PLoS Comput. Biol. , vol.9
    • Portella, G.1    Battistini, F.2    Orozco, M.3
  • 107
    • 84874416243 scopus 로고    scopus 로고
    • Most methylation-susceptible DNA sequences in human embryonic stem cells undergo a change in conformation or flexibility upon methylation
    • Y. Shimooka, J. Nishikawa, and T. Ohyama Most methylation-susceptible DNA sequences in human embryonic stem cells undergo a change in conformation or flexibility upon methylation Biochemistry 52 2013 1344 1353
    • (2013) Biochemistry , vol.52 , pp. 1344-1353
    • Shimooka, Y.1    Nishikawa, J.2    Ohyama, T.3
  • 108
    • 0036306349 scopus 로고    scopus 로고
    • Bending and flexibility of methylated and unmethylated EcoRI DNA
    • D. Nathan, and D.M. Crothers Bending and flexibility of methylated and unmethylated EcoRI DNA J. Mol. Biol. 316 2002 7 17
    • (2002) J. Mol. Biol. , vol.316 , pp. 7-17
    • Nathan, D.1    Crothers, D.M.2
  • 110
    • 0036922909 scopus 로고    scopus 로고
    • Structural effects of cytosine methylation on DNA sugar pucker studied by FTIR
    • M. Banyay, and A. Graslund Structural effects of cytosine methylation on DNA sugar pucker studied by FTIR J. Mol. Biol. 324 2002 667 676
    • (2002) J. Mol. Biol. , vol.324 , pp. 667-676
    • Banyay, M.1    Graslund, A.2
  • 111
    • 0026808756 scopus 로고
    • Cytosine methylation can induce local distortions in the structure of duplex DNA
    • Y. Hodgesgarcia, and P.J. Hagerman Cytosine methylation can induce local distortions in the structure of duplex DNA Biochemistry 31 1992 7595 7599
    • (1992) Biochemistry , vol.31 , pp. 7595-7599
    • Hodgesgarcia, Y.1    Hagerman, P.J.2
  • 112
    • 0028840147 scopus 로고
    • Investigation of the influence of cytosine methylation on DNA flexibility
    • Y. Hodgesgarcia, and P.J. Hagerman Investigation of the influence of cytosine methylation on DNA flexibility J. Biol. Chem. 270 1995 197 201
    • (1995) J. Biol. Chem. , vol.270 , pp. 197-201
    • Hodgesgarcia, Y.1    Hagerman, P.J.2
  • 113
    • 0035369057 scopus 로고    scopus 로고
    • Impact of CpG methylation on structure, dynamics and solvation of cAMP DNA responsive element
    • S. Derreumaux, M. Chaoui, G. Tevanian, and S. Fermandjian Impact of CpG methylation on structure, dynamics and solvation of cAMP DNA responsive element Nucleic Acids Res. 29 2001 2314 2326
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2314-2326
    • Derreumaux, S.1    Chaoui, M.2    Tevanian, G.3    Fermandjian, S.4
  • 114
    • 84910045456 scopus 로고    scopus 로고
    • Enhanced sampling simulations of DNA step parameters
    • submitted for publication
    • A. Karolak, and A. van der Vaart Enhanced sampling simulations of DNA step parameters J. Comput. Chem. 2014 (submitted for publication)
    • (2014) J. Comput. Chem.
    • Karolak, A.1    Van Der Vaart, A.2
  • 115
    • 0019544304 scopus 로고
    • Effects of methylation on a synthetic polynucleotide - The B-Z transition in poly(dG-m5dC).poly(dG-m5dC)
    • M. Behe, and G. Felsenfeld Effects of methylation on a synthetic polynucleotide - the B-Z transition in poly(dG-m5dC).poly(dG-m5dC) Proc. Natl. Acad. Sci. U. S. A. Biol. Sci. 78 1981 1619 1623
    • (1981) Proc. Natl. Acad. Sci. U. S. A. Biol. Sci. , vol.78 , pp. 1619-1623
    • Behe, M.1    Felsenfeld, G.2
  • 116
    • 33751253464 scopus 로고    scopus 로고
    • Enthalpy of the B-to-Z conformational transition of a DNA oligonucleotide determined by isothermal titration calorimetry
    • J.M. Ferreira, and R.D. Sheardy Enthalpy of the B-to-Z conformational transition of a DNA oligonucleotide determined by isothermal titration calorimetry Biophys. J. 91 2006 3383 3389
    • (2006) Biophys. J. , vol.91 , pp. 3383-3389
    • Ferreira, J.M.1    Sheardy, R.D.2
  • 117
    • 78650879122 scopus 로고    scopus 로고
    • CGG repeats associated with fragile X chromosome form left-handed Z-DNA structure
    • D. Renciuk, J. Kypr, and M. Vorlickova CGG repeats associated with fragile X chromosome form left-handed Z-DNA structure Biopolymers 95 2011 174 181
    • (2011) Biopolymers , vol.95 , pp. 174-181
    • Renciuk, D.1    Kypr, J.2    Vorlickova, M.3
  • 118
    • 0030754556 scopus 로고    scopus 로고
    • Methylation of the Z-DNA decamer d(GC)(5) potentiates the formation of A-DNA: Crystal structure of d(Gm(5)CGm(5)CGCGCGC)
    • D.B. Tippin, B. Ramakrishnan, and M. Sundaralingam Methylation of the Z-DNA decamer d(GC)(5) potentiates the formation of A-DNA: Crystal structure of d(Gm(5)CGm(5)CGCGCGC) J. Mol. Biol. 270 1997 247 258
    • (1997) J. Mol. Biol. , vol.270 , pp. 247-258
    • Tippin, D.B.1    Ramakrishnan, B.2    Sundaralingam, M.3
  • 121
    • 0028919503 scopus 로고
    • Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor
    • J.D. Parvin, R.J. McCormick, P.A. Sharp, and D.E. Fisher Pre-bending of a promoter sequence enhances affinity for the TATA-binding factor Nature 373 1995 724 727
    • (1995) Nature , vol.373 , pp. 724-727
    • Parvin, J.D.1    McCormick, R.J.2    Sharp, P.A.3    Fisher, D.E.4
  • 123
    • 0031010691 scopus 로고    scopus 로고
    • Prebending the estrogen response element destabilizes binding of the estrogen receptor DNA binding domain
    • J. Kim, G. deHaan, A.M. Nardulli, and D.J. Shapiro Prebending the estrogen response element destabilizes binding of the estrogen receptor DNA binding domain Mol. Cell. Biol. 17 1997 3173 3180
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3173-3180
    • Kim, J.1    DeHaan, G.2    Nardulli, A.M.3    Shapiro, D.J.4
  • 124
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • D.E. Koshland Application of a theory of enzyme specificity to protein synthesis Proc. Natl. Acad. Sci. U. S. A. 44 1958 98 104
    • (1958) Proc. Natl. Acad. Sci. U. S. A. , vol.44 , pp. 98-104
    • Koshland, D.E.1
  • 125
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • D.D. Boehr, R. Nussinov, and P.E. Wright The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5 2009 789 796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 126
    • 77957754309 scopus 로고    scopus 로고
    • Enzyme dynamics point to stepwise conformational selection in catalysis
    • B.Y. Ma, and R. Nussinov Enzyme dynamics point to stepwise conformational selection in catalysis Curr. Opin. Chem. Biol. 14 2010 652 659
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 652-659
    • Ma, B.Y.1    Nussinov, R.2
  • 127
    • 84881610902 scopus 로고    scopus 로고
    • DNA binding and bending by Sac7d is stepwise
    • J. Spiriti, and A. van der Vaart DNA binding and bending by Sac7d is stepwise ChemBioChem 14 2013 1434 1437
    • (2013) ChemBioChem , vol.14 , pp. 1434-1437
    • Spiriti, J.1    Van Der Vaart, A.2
  • 128
    • 84890076953 scopus 로고    scopus 로고
    • Conformational dynamics of an ATP-binding DNA aptamer: A single-molecule study
    • T. Xia, J. Yuan, and X. Fang Conformational dynamics of an ATP-binding DNA aptamer: a single-molecule study J. Phys. Chem. B 117 2013 14994 15003
    • (2013) J. Phys. Chem. B , vol.117 , pp. 14994-15003
    • Xia, T.1    Yuan, J.2    Fang, X.3
  • 129
    • 79851474946 scopus 로고    scopus 로고
    • Intrinsic Z-DNA is stabilized by the conformational selection mechanism of Z-DNA-binding proteins
    • S. Bae, D. Kim, K.K. Kim, Y.-G. Kim, and S. Hohng Intrinsic Z-DNA is stabilized by the conformational selection mechanism of Z-DNA-binding proteins J. Am. Chem. Soc. 133 2011 668 671
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 668-671
    • Bae, S.1    Kim, D.2    Kim, K.K.3    Kim, Y.-G.4    Hohng, S.5
  • 130
    • 0032514675 scopus 로고    scopus 로고
    • RecA binding to a single double-stranded DNA molecule: A possible role of DNA conformational fluctuations
    • J.F. Leger, J. Robert, L. Bourdieu, D. Chatenay, and J.F. Marko RecA binding to a single double-stranded DNA molecule: a possible role of DNA conformational fluctuations Proc. Natl. Acad. Sci. U. S. A. 95 1998 12295 12299
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12295-12299
    • Leger, J.F.1    Robert, J.2    Bourdieu, L.3    Chatenay, D.4    Marko, J.F.5
  • 131
    • 33845500268 scopus 로고    scopus 로고
    • Stepwise binding and bending of DNA by Escherichia coli integration host factor
    • S. Sugimura, and D.M. Crothers Stepwise binding and bending of DNA by Escherichia coli integration host factor Proc. Natl. Acad. Sci. U. S. A. 103 2006 18510 18514
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 18510-18514
    • Sugimura, S.1    Crothers, D.M.2
  • 133
    • 44949085459 scopus 로고    scopus 로고
    • New insights into the transition pathway from nonspecific to specific complex of DNA with Escherichia coli integration host factor
    • P. Vivas, S.V. Kuznetsov, and A. Ansari New insights into the transition pathway from nonspecific to specific complex of DNA with Escherichia coli integration host factor J. Phys. Chem. B 112 2008 5997 6007
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5997-6007
    • Vivas, P.1    Kuznetsov, S.V.2    Ansari, A.3
  • 135
    • 0029943025 scopus 로고    scopus 로고
    • Simultaneous binding and bending of promoter DNA by the TATA binding protein: Real time kinetic measurements
    • K.M. Parkhurst, M. Brenowitz, and L.J. Parkhurst Simultaneous binding and bending of promoter DNA by the TATA binding protein: real time kinetic measurements Biochemistry 35 1996 7459 7465
    • (1996) Biochemistry , vol.35 , pp. 7459-7465
    • Parkhurst, K.M.1    Brenowitz, M.2    Parkhurst, L.J.3
  • 136
    • 0033603388 scopus 로고    scopus 로고
    • Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex
    • K.M. Parkhurst, R.M. Richards, M. Brenowitz, and L.J. Parkhurst Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex J. Mol. Biol. 289 1999 1327 1341
    • (1999) J. Mol. Biol. , vol.289 , pp. 1327-1341
    • Parkhurst, K.M.1    Richards, R.M.2    Brenowitz, M.3    Parkhurst, L.J.4
  • 137
    • 0035839638 scopus 로고    scopus 로고
    • Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters
    • R.M. Powell, K.M. Parkhurst, M. Brenowitz, and L.J. Parkhurst Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters J. Biol. Chem. 276 2001 29782 29791
    • (2001) J. Biol. Chem. , vol.276 , pp. 29782-29791
    • Powell, R.M.1    Parkhurst, K.M.2    Brenowitz, M.3    Parkhurst, L.J.4
  • 138
    • 64349107263 scopus 로고    scopus 로고
    • The TATA-binding protein core domain in solution variably bends TATA sequences via a three-step binding mechanism
    • R.F. Delgadillo, J.E. Whittington, L.K. Parkhurst, and L.J. Parkhurst The TATA-binding protein core domain in solution variably bends TATA sequences via a three-step binding mechanism Biochemistry 48 2009 1801 1809
    • (2009) Biochemistry , vol.48 , pp. 1801-1809
    • Delgadillo, R.F.1    Whittington, J.E.2    Parkhurst, L.K.3    Parkhurst, L.J.4
  • 139
    • 0346220020 scopus 로고    scopus 로고
    • Simultaneous DNA binding and bending by EcoRV endonuclease observed by real-time fluorescence
    • D.A. Hiller, J.M. Fogg, A.M. Martin, J.M. Beechem, N.O. Reich, and J.J. Perona Simultaneous DNA binding and bending by EcoRV endonuclease observed by real-time fluorescence Biochemistry 42 2003 14375 14385
    • (2003) Biochemistry , vol.42 , pp. 14375-14385
    • Hiller, D.A.1    Fogg, J.M.2    Martin, A.M.3    Beechem, J.M.4    Reich, N.O.5    Perona, J.J.6
  • 140
    • 0034986024 scopus 로고    scopus 로고
    • DNA-binding proteins Sac7d and Sso7d from Sulfolobus
    • S.P. Edmondson, and J.W. Shriver DNA-binding proteins Sac7d and Sso7d from Sulfolobus Methods Enzymol. 334 2001 129 145
    • (2001) Methods Enzymol. , vol.334 , pp. 129-145
    • Edmondson, S.P.1    Shriver, J.W.2
  • 141
    • 84896393714 scopus 로고    scopus 로고
    • RevErbα preferentially deforms DNA by induced fit
    • Y.H. Chung, and A. van der Vaart RevErbα preferentially deforms DNA by induced fit ChemBioChem 15 2014 643 646
    • (2014) ChemBioChem , vol.15 , pp. 643-646
    • Chung, Y.H.1    Van Der Vaart, A.2
  • 142
    • 17844406392 scopus 로고    scopus 로고
    • Induced fit and the entropy of structural adaptation in the complexation of CAP and lambda-repressor with cognate DNA sequences
    • S.B. Dixit, D.Q. Andrews, and D.L. Beveridge Induced fit and the entropy of structural adaptation in the complexation of CAP and lambda-repressor with cognate DNA sequences Biophys. J. 88 2005 3147 3157
    • (2005) Biophys. J. , vol.88 , pp. 3147-3157
    • Dixit, S.B.1    Andrews, D.Q.2    Beveridge, D.L.3
  • 143
    • 84864462749 scopus 로고    scopus 로고
    • Conformational selection or induced fit? A critical appraisal of the kinetic mechanism
    • A.D. Vogt, and E. Di Cera Conformational selection or induced fit? A critical appraisal of the kinetic mechanism Biochemistry 51 2012 5894 5902
    • (2012) Biochemistry , vol.51 , pp. 5894-5902
    • Vogt, A.D.1    Di Cera, E.2
  • 144
    • 69549120472 scopus 로고    scopus 로고
    • Conformational selection or induced fit: A flux description of reaction mechanism
    • G.G. Hammes, Y.-C. Chang, and T.G. Oas Conformational selection or induced fit: a flux description of reaction mechanism Proc. Natl. Acad. Sci. U. S. A. 106 2009 13737 13741
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13737-13741
    • Hammes, G.G.1    Chang, Y.-C.2    Oas, T.G.3
  • 146
    • 33746786029 scopus 로고    scopus 로고
    • DNA recognition by the Brinker repressor - An extreme case of coupling between binding and folding
    • F. Cordier, B. Hartmann, M. Rogowski, M. Affolter, and S. Grzesiek DNA recognition by the Brinker repressor - An extreme case of coupling between binding and folding J. Mol. Biol. 361 2006 659 672
    • (2006) J. Mol. Biol. , vol.361 , pp. 659-672
    • Cordier, F.1    Hartmann, B.2    Rogowski, M.3    Affolter, M.4    Grzesiek, S.5
  • 147
    • 53949123299 scopus 로고    scopus 로고
    • Characterization of the papillomavirus alpha(1)E2 peptide unfolded to folded transition upon DNA binding
    • G.M. Giesel, L.M.T.R. Lima, J. Faber-Barata, J.A. Guimaraes, and H. Verli Characterization of the papillomavirus alpha(1)E2 peptide unfolded to folded transition upon DNA binding FEBS Lett. 582 2008 3619 3624
    • (2008) FEBS Lett. , vol.582 , pp. 3619-3624
    • Giesel, G.M.1    Lima, L.M.T.R.2    Faber-Barata, J.3    Guimaraes, J.A.4    Verli, H.5
  • 148
    • 84887831600 scopus 로고    scopus 로고
    • Conformational dynamics of the partially disordered yeast transcription factor GCN4
    • P. Robustelli, N. Trbovic, R.A. Friesner, and A.G. Palmer III Conformational dynamics of the partially disordered yeast transcription factor GCN4 J. Chem. Theory Comput. 9 2013 5190 5200
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 5190-5200
    • Robustelli, P.1    Trbovic, N.2    Friesner, R.A.3    Palmer, A.G.4
  • 149
    • 62649113018 scopus 로고    scopus 로고
    • Correlated motions and interactions at the onset of the DNA-induced partial unfolding of Ets-1
    • H. Kamberaj, and A. van der Vaart Correlated motions and interactions at the onset of the DNA-induced partial unfolding of Ets-1 Biophys. J. 96 2009 1307 1317
    • (2009) Biophys. J. , vol.96 , pp. 1307-1317
    • Kamberaj, H.1    Van Der Vaart, A.2
  • 150
    • 0029048413 scopus 로고
    • Structure of Bam HI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • M. Newman, T. Strzelecka, L. Dorner, I. Schildkraut, and A. Aggarwal Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding Science 269 1995 656
    • (1995) Science , vol.269 , pp. 656
    • Newman, M.1    Strzelecka, T.2    Dorner, L.3    Schildkraut, I.4    Aggarwal, A.5
  • 151
    • 0028874393 scopus 로고
    • Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an α helix
    • J.M. Petersen, J.J. Skalicky, L.W. Donaldson, L.P. McIntosh, T. Alber, and B.J. Graves Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an α helix Science 269 1995 1866 1869
    • (1995) Science , vol.269 , pp. 1866-1869
    • Petersen, J.M.1    Skalicky, J.J.2    Donaldson, L.W.3    McIntosh, L.P.4    Alber, T.5    Graves, B.J.6
  • 153
    • 0347928848 scopus 로고    scopus 로고
    • Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships
    • C.W. Garvie, M.A. Pufall, B.J. Graves, and C. Wolberger Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships J. Biol. Chem. 277 2002 45529 45536
    • (2002) J. Biol. Chem. , vol.277 , pp. 45529-45536
    • Garvie, C.W.1    Pufall, M.A.2    Graves, B.J.3    Wolberger, C.4
  • 154
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: Modular effectors of cellular regulation
    • M.A. Pufall, and B.J. Graves Autoinhibitory domains: modular effectors of cellular regulation Annu. Rev. Cell Dev. Biol. 18 2002 421 462
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 155
    • 84860755238 scopus 로고    scopus 로고
    • Importance of local interactions for the stability of inhibitory helix 1 in apo Ets-1
    • A. Karolak, and A. van der Vaart Importance of local interactions for the stability of inhibitory helix 1 in apo Ets-1 Biophys. Chem. 165-166 2012 74 78
    • (2012) Biophys. Chem. , vol.165-166 , pp. 74-78
    • Karolak, A.1    Van Der Vaart, A.2
  • 156
    • 12944275674 scopus 로고    scopus 로고
    • Measuring information transfer
    • T. Schreiber Measuring information transfer Phys. Rev. Lett. 85 2000 461 464
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 461-464
    • Schreiber, T.1
  • 157
    • 70350035647 scopus 로고    scopus 로고
    • Extracting the causality of correlated motions from molecular dynamics simulations
    • H. Kamberaj, and A. van der Vaart Extracting the causality of correlated motions from molecular dynamics simulations Biophys. J. 97 2009 1747 1755
    • (2009) Biophys. J. , vol.97 , pp. 1747-1755
    • Kamberaj, H.1    Van Der Vaart, A.2
  • 158
    • 77649111696 scopus 로고    scopus 로고
    • Insights into the sliding movement of the lac repressor nonspecifically bound to DNA
    • S. Furini, C. Domene, and S. Cavalcanti Insights into the sliding movement of the lac repressor nonspecifically bound to DNA J. Phys. Chem. B 114 2010 2238 2245
    • (2010) J. Phys. Chem. B , vol.114 , pp. 2238-2245
    • Furini, S.1    Domene, C.2    Cavalcanti, S.3
  • 161
    • 84876554311 scopus 로고    scopus 로고
    • DNA-recognition process described by MD simulations of the lactose repressor protein on a specific and a non-specific DNA sequence
    • S. Furini, P. Barbini, and C. Domene DNA-recognition process described by MD simulations of the lactose repressor protein on a specific and a non-specific DNA sequence Nucleic Acids Res. 41 2013 3963 3972
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3963-3972
    • Furini, S.1    Barbini, P.2    Domene, C.3
  • 162
    • 0030596509 scopus 로고    scopus 로고
    • Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: Change of tertiary structure upon binding to the lac operator
    • M. Slijper, A.M.J.J. Bonvin, R. Boelens, and R. Kaptein Refined structure of lac repressor headpiece (1-56) determined by relaxation matrix calculations from 2D and 3D NOE data: change of tertiary structure upon binding to the lac operator J. Mol. Biol. 259 1996 761 773
    • (1996) J. Mol. Biol. , vol.259 , pp. 761-773
    • Slijper, M.1    Bonvin, A.M.J.J.2    Boelens, R.3    Kaptein, R.4
  • 163
    • 0037124326 scopus 로고    scopus 로고
    • Plasticity in protein-DNA recognition: Lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain
    • C.G. Kalodimos, A.M.J.J. Bonvin, R.K. Salinas, R. Wechselberger, R. Boelens, and R. Kaptein Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain EMBO J. 21 2002 2866 2876
    • (2002) EMBO J. , vol.21 , pp. 2866-2876
    • Kalodimos, C.G.1    Bonvin, A.M.J.J.2    Salinas, R.K.3    Wechselberger, R.4    Boelens, R.5    Kaptein, R.6
  • 164
    • 4344581629 scopus 로고    scopus 로고
    • Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the lac repressor system
    • C.G. Kalodimos, R. Boelens, and R. Kaptein Toward an integrated model of protein-DNA recognition as inferred from NMR studies on the lac repressor system Chem. Rev. 104 2004 3567 3586
    • (2004) Chem. Rev. , vol.104 , pp. 3567-3586
    • Kalodimos, C.G.1    Boelens, R.2    Kaptein, R.3
  • 165
    • 84883411381 scopus 로고    scopus 로고
    • Binding polymorphism in the DNA bound state of the Pdx1 homeodomain
    • V. Babin, D. Wang, R.B. Rose, and C. Sagui Binding polymorphism in the DNA bound state of the Pdx1 homeodomain PLoS Comput. Biol. 9 2013
    • (2013) PLoS Comput. Biol. , vol.9
    • Babin, V.1    Wang, D.2    Rose, R.B.3    Sagui, C.4
  • 166
    • 33947408340 scopus 로고    scopus 로고
    • Structural basis for induced fit mechanisms in DNA recognition by the Pdx1 homeodomain
    • A. Longo, G.P. Guanga, and R.B. Rose Structural basis for induced fit mechanisms in DNA recognition by the Pdx1 homeodomain Biochemistry 46 2007 2948 2957
    • (2007) Biochemistry , vol.46 , pp. 2948-2957
    • Longo, A.1    Guanga, G.P.2    Rose, R.B.3
  • 167
    • 84856750734 scopus 로고    scopus 로고
    • The natural DNA bending angle in the lac repressor headpiece-O1 operator complex is determined by protein-DNA contacts and water release
    • D. Barr, and A. van der Vaart The natural DNA bending angle in the lac repressor headpiece-O1 operator complex is determined by protein-DNA contacts and water release Phys. Chem. Chem. Phys. 14 2012 2070 2077
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 2070-2077
    • Barr, D.1    Van Der Vaart, A.2
  • 169
    • 18744391399 scopus 로고    scopus 로고
    • Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation
    • E. Villa, A. Balaeff, and K. Schulten Structural dynamics of the lac repressor-DNA complex revealed by a multiscale simulation Proc. Natl. Acad. Sci. U. S. A. 102 2005 6783 6788
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6783-6788
    • Villa, E.1    Balaeff, A.2    Schulten, K.3
  • 170
    • 67649447246 scopus 로고    scopus 로고
    • Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor
    • S. Goffinont, M. Davidkova, and M. Spotheim-Maurizot Radiation-induced tetramer-to-dimer transition of Escherichia coli lactose repressor Biochem. Biophys. Res. Commun. 386 2009 300 304
    • (2009) Biochem. Biophys. Res. Commun. , vol.386 , pp. 300-304
    • Goffinont, S.1    Davidkova, M.2    Spotheim-Maurizot, M.3
  • 173
    • 20544460658 scopus 로고    scopus 로고
    • Protein-DNA recognition patterns and predictions
    • A. Sarai, and H. Kono Protein-DNA recognition patterns and predictions Annu. Rev. Biophys. Biomol. Struct. 34 2005 379 398
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 379-398
    • Sarai, A.1    Kono, H.2
  • 175
    • 0028988416 scopus 로고
    • Mg2 + binding to the active-site of EcoRV endonuclease - A crystallographic study of complexes with substrate and product DNA at 2-Ångstrom resolution
    • D. Kostrewa, and F.K. Winkler Mg2 + binding to the active-site of EcoRV endonuclease - A crystallographic study of complexes with substrate and product DNA at 2-Ångstrom resolution Biochemistry 34 1995 683 696
    • (1995) Biochemistry , vol.34 , pp. 683-696
    • Kostrewa, D.1    Winkler, F.K.2
  • 176
    • 0032972857 scopus 로고    scopus 로고
    • Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease
    • A.M. Martin, M.D. Sam, N.O. Reich, and J.J. Perona Structural and energetic origins of indirect readout in site-specific DNA cleavage by a restriction endonuclease Nat. Struct. Biol. 6 1999 269 277
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 269-277
    • Martin, A.M.1    Sam, M.D.2    Reich, N.O.3    Perona, J.J.4
  • 177
    • 77955267122 scopus 로고    scopus 로고
    • Mechanism of DNA recognition by the restriction enzyme EcoRV
    • M. Zahran, I. Daidone, J.C. Smith, and P. Imhof Mechanism of DNA recognition by the restriction enzyme EcoRV J. Mol. Biol. 401 2010 415 432
    • (2010) J. Mol. Biol. , vol.401 , pp. 415-432
    • Zahran, M.1    Daidone, I.2    Smith, J.C.3    Imhof, P.4
  • 178
    • 49149090309 scopus 로고    scopus 로고
    • P53-induced DNA bending: The interplay between p53-ONA and p53-p53 interactions
    • Y. Pan, and R. Nussinov p53-induced DNA bending: the interplay between p53-ONA and p53-p53 interactions J. Phys. Chem. B 112 2008 6716 6724
    • (2008) J. Phys. Chem. B , vol.112 , pp. 6716-6724
    • Pan, Y.1    Nussinov, R.2
  • 179
  • 180
    • 33746776203 scopus 로고    scopus 로고
    • Minor groove deformability of DNA: A molecular dynamics free energy simulation study
    • M. Zacharias Minor groove deformability of DNA: a molecular dynamics free energy simulation study Biophys. J. 91 2006 882 891
    • (2006) Biophys. J. , vol.91 , pp. 882-891
    • Zacharias, M.1
  • 181
    • 52249100539 scopus 로고    scopus 로고
    • Investigation of transcription factor Ndt80 affinity differences for wild type and mutant DNA: A molecular dynamics study
    • K. Hart, and L. Nilsson Investigation of transcription factor Ndt80 affinity differences for wild type and mutant DNA: a molecular dynamics study Proteins Struct. Funct. Bioinform. 73 2008 325 337
    • (2008) Proteins Struct. Funct. Bioinform. , vol.73 , pp. 325-337
    • Hart, K.1    Nilsson, L.2


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