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Volumn 44, Issue 51, 2005, Pages 16988-16997

Hydration changes in the association of Hoechst 33258 with DNA

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; DNA; HYDRATION; MOLECULAR WEIGHT; OSMOSIS; TITRATION; WATER;

EID: 29344435546     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051769x     Document Type: Article
Times cited : (48)

References (88)
  • 3
    • 0034951136 scopus 로고    scopus 로고
    • DNA minor-groove recognition by small molecules
    • Neidle, S. (2001) DNA minor-groove recognition by small molecules, Nat. Prod. Rep. 18, 291-309.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 291-309
    • Neidle, S.1
  • 5
    • 0035042617 scopus 로고    scopus 로고
    • Recent developments in sequence selective minor groove DNA effectors
    • Reddy, B. S., Sharma, S. K., and Lown, J. W. (2001) Recent developments in sequence selective minor groove DNA effectors, Curr. Med. Chem. 8, 475-508.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 475-508
    • Reddy, B.S.1    Sharma, S.K.2    Lown, J.W.3
  • 6
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record, M. T., Jr., Anderson, C. F., and Lohman, T. M. (1978) Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity, Q. Rev. Biophys. 11, 103-178.
    • (1978) Q. Rev. Biophys. , vol.11 , pp. 103-178
    • Record Jr., M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 7
    • 0001076529 scopus 로고
    • Structure and function of restriction endonucleases
    • Rosenberg, J. M. (1991) Structure and function of restriction endonucleases, Curr. Opin. Struct. Biol. 1, 104-113.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 104-113
    • Rosenberg, J.M.1
  • 8
    • 3543040694 scopus 로고    scopus 로고
    • A molecular thermodynamic view of DNA-drug interactions: A case study of 25 minor-groove binders
    • Shaikh, S. A., Ahmed, S. R., and Jayaram, B. (2004) A molecular thermodynamic view of DNA-drug interactions: a case study of 25 minor-groove binders, Arch. Biochem. Biophys. 429, 81-99.
    • (2004) Arch. Biochem. Biophys. , vol.429 , pp. 81-99
    • Shaikh, S.A.1    Ahmed, S.R.2    Jayaram, B.3
  • 9
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and Record, M. T., Jr. (1994) Coupling of local folding to site-specific binding of proteins to DNA, Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 12
    • 0030466444 scopus 로고    scopus 로고
    • Just add water! the effect of water on the specificity of protein-ligand binding sites and its potential application to drug design
    • Ladbury, J. E. (1996) Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design, Chem. Biol. 3, 973-980.
    • (1996) Chem. Biol. , vol.3 , pp. 973-980
    • Ladbury, J.E.1
  • 13
    • 0031047683 scopus 로고    scopus 로고
    • The role of water in protein-DNA interactions
    • Schwabe, J. W. (1997) The role of water in protein-DNA interactions, Curr. Opin. Struct. Biol. 7, 126-134.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 126-134
    • Schwabe, J.W.1
  • 14
    • 0037337378 scopus 로고    scopus 로고
    • Sequence-specific minor groove binding by bis-benzimidazoles: Water molecules in ligand recognition
    • Bailly, C., Chessari, G., Carrasco, C., Joubert, A., Mann, J., Wilson, W. D., and Neidle, S. (2003) Sequence-specific minor groove binding by bis-benzimidazoles: water molecules in ligand recognition, Nucleic Acids Res. 31, 1514-1524.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1514-1524
    • Bailly, C.1    Chessari, G.2    Carrasco, C.3    Joubert, A.4    Mann, J.5    Wilson, W.D.6    Neidle, S.7
  • 15
    • 0032788299 scopus 로고    scopus 로고
    • 2 complex determined by NMR and molecular dynamics simulations in solution
    • 2 complex determined by NMR and molecular dynamics simulations in solution, J. Mol. Biol. 290, 699-716.
    • (1999) J. Mol. Biol. , vol.290 , pp. 699-716
    • Williams, H.E.L.1    Searle, M.S.2
  • 16
    • 14744268745 scopus 로고    scopus 로고
    • Heat capacity effects in protein folding and ligand binding: A re-evaluation of the role of water in biomolecular thermodynamics
    • Cooper, A. (2005) Heat capacity effects in protein folding and ligand binding: a re-evaluation of the role of water in biomolecular thermodynamics, Biophys. Chem. 115, 89-97.
    • (2005) Biophys. Chem. , vol.115 , pp. 89-97
    • Cooper, A.1
  • 17
    • 0026535070 scopus 로고
    • Protein solvation in allosteric regulation: A water effect on hemoglobin
    • (a) Colombo, M. F., Rau, D. C., and Parsegian, V. A. (1992) Protein solvation in allosteric regulation: a water effect on hemoglobin, Science 256, 655-659;
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, V.A.3
  • 18
    • 0026530285 scopus 로고
    • Raising water to new heights
    • (b) Rand, R. P. (1992) Raising water to new heights, Science 256, 618.
    • (1992) Science , vol.256 , pp. 618
    • Rand, R.P.1
  • 19
    • 0000137680 scopus 로고    scopus 로고
    • Volumetric properties of nucleic acids
    • (a) Chalikian, T. V., and Breslauer, K. J. (1998) Volumetric properties of nucleic acids, Biopolymers 48, 264-280;
    • (1998) Biopolymers , vol.48 , pp. 264-280
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 21
    • 0029144073 scopus 로고
    • Hydrostatic and osmotic pressure as tools to study macromolecular recognition
    • Robinson, C. R., and Sligar, S. G. (1995) Hydrostatic and osmotic pressure as tools to study macromolecular recognition, Methods Enzymol. 259, 395-427.
    • (1995) Methods Enzymol. , vol.259 , pp. 395-427
    • Robinson, C.R.1    Sligar, S.G.2
  • 22
    • 0842342617 scopus 로고    scopus 로고
    • Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments
    • Shimizu, S. (2004) Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments. Proc. Natl. Acad. Sci. U.S.A. 101, 1195-1199.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1195-1199
    • Shimizu, S.1
  • 23
    • 0031571628 scopus 로고    scopus 로고
    • Specific binding of Hoechst 33258 to the d(CGCAAATTTGCG)2 duplex: Calorimetric and spectroscopic studies
    • Haq, I., Ladbury, J. E., Chowdhry, B. Z., Jenkins, T. C., and Chaires, J. B. (1997) Specific binding of Hoechst 33258 to the d(CGCAAATTTGCG)2 duplex: calorimetric and spectroscopic studies, J. Mol. Biol. 271, 244-257.
    • (1997) J. Mol. Biol. , vol.271 , pp. 244-257
    • Haq, I.1    Ladbury, J.E.2    Chowdhry, B.Z.3    Jenkins, T.C.4    Chaires, J.B.5
  • 24
    • 0036647051 scopus 로고    scopus 로고
    • Thermodynamics of drug-DNA interactions
    • Haq, I. (2002) Thermodynamics of drug-DNA interactions, Arch. Biochem. Biophys. 403, 1-15.
    • (2002) Arch. Biochem. Biophys. , vol.403 , pp. 1-15
    • Haq, I.1
  • 25
    • 0034536719 scopus 로고    scopus 로고
    • Thermodynamics of nucleic acids and their interactions with ligands
    • Lane, A. N., and Jenkins, T. C. (2000) Thermodynamics of nucleic acids and their interactions with ligands, Q. Rev. Biophys. 33, 255-306.
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 255-306
    • Lane, A.N.1    Jenkins, T.C.2
  • 26
    • 4744338722 scopus 로고    scopus 로고
    • The extended interface: Measuring non-local effects in biomolecular interactions
    • Ladbury, J. E., and Williams, M. A. (2004) The extended interface: measuring non-local effects in biomolecular interactions, Curr. Opin. Struct. Bio. 14, 562-569.
    • (2004) Curr. Opin. Struct. Bio. , vol.14 , pp. 562-569
    • Ladbury, J.E.1    Williams, M.A.2
  • 27
    • 0025786551 scopus 로고
    • Molecular recognition between ligands and nucleic acids: DNA binding characteristics of analogues of Hoechst 33258 designed to exhibit altered base and sequence recognition
    • Rao, K. E., and Lown, J. W. (1991) Molecular recognition between ligands and nucleic acids: DNA binding characteristics of analogues of Hoechst 33258 designed to exhibit altered base and sequence recognition, Chem. Res. Toxicol. 4, 661-669.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 661-669
    • Rao, K.E.1    Lown, J.W.2
  • 28
    • 0033119666 scopus 로고    scopus 로고
    • DNA minor groove recognition by bis-benzimidazole analogues of Hoechst 33258: Insights into structure-DNA affinity relationships assessed by fluorescence titration measurements
    • Bostock-Smith, C., and Searle, M. (1999) DNA minor groove recognition by bis-benzimidazole analogues of Hoechst 33258: insights into structure-DNA affinity relationships assessed by fluorescence titration measurements, Nucleic Acids Res. 27, 1619-1624.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1619-1624
    • Bostock-Smith, C.1    Searle, M.2
  • 29
    • 0023626977 scopus 로고
    • Binding of Hoechst 33258 to the minor groove of B-DNA
    • Pjura, P. E., Grzeskowiak, K., and Dickerson, R. E. (1987) Binding of Hoechst 33258 to the minor groove of B-DNA, J. Mol. Biol. 197, 257-271.
    • (1987) J. Mol. Biol. , vol.197 , pp. 257-271
    • Pjura, P.E.1    Grzeskowiak, K.2    Dickerson, R.E.3
  • 30
    • 0025885778 scopus 로고
    • Low-temperature crystallographic analyses of the binding of Hoechst 33258 to the double-helical DNA dodecamer C-G-C-G-A-A-T-T-C-G-C-G
    • Quintana, J. R., Lipanov, A. A., and Dickerson, R. E. (1991) Low-temperature crystallographic analyses of the binding of Hoechst 33258 to the double-helical DNA dodecamer C-G-C-G-A-A-T-T-C-G-C-G, Biochemistry 30, 10294-10306.
    • (1991) Biochemistry , vol.30 , pp. 10294-10306
    • Quintana, J.R.1    Lipanov, A.A.2    Dickerson, R.E.3
  • 31
    • 0031574354 scopus 로고    scopus 로고
    • Interaction of minor groove binding ligands with long at tracts
    • Abu-Daya, A., and Fox, K. (1997) Interaction of minor groove binding ligands with long AT tracts, Nucleic Acids Res. 25, 4962-4969.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4962-4969
    • Abu-Daya, A.1    Fox, K.2
  • 32
    • 0034833710 scopus 로고    scopus 로고
    • A simple, high-resolution method for establishing DNA binding affinity and sequence selectivity
    • Boger, D. L., Fink, B. E., Brunette, S. R., Tse, W. C., and Hedrick, M. P. (2001) A simple, high-resolution method for establishing DNA binding affinity and sequence selectivity, J. Am. Chem. Soc. 123, 5878-5891.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5878-5891
    • Boger, D.L.1    Fink, B.E.2    Brunette, S.R.3    Tse, W.C.4    Hedrick, M.P.5
  • 33
    • 0036306118 scopus 로고    scopus 로고
    • Base-sequence specificity of Hoechst 33258 and DAPI binding to five (A/T)4 DNA sites with kinetic evidence for more than one high-affinity Hoechst 33258-AATT complex
    • Breusegem, S. Y., Clegg, R. M., and Loontiens, F. G. (2002) Base-sequence specificity of Hoechst 33258 and DAPI binding to five (A/T)4 DNA sites with kinetic evidence for more than one high-affinity Hoechst 33258-AATT complex, J. Mol. Biol. 315, 1049-1061.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1049-1061
    • Breusegem, S.Y.1    Clegg, R.M.2    Loontiens, F.G.3
  • 34
    • 0025006448 scopus 로고
    • Binding characteristics of Hoechst 33258 with calf thymus DNA, poly[d(A-T)] and d(CCGGAATTCCGG): Multiple stoichiometries and determination of tight binding with a wide spectrum of site affinities
    • Loontiens, F. G., Regenfuss, P., Zechel, A., Dumortier, L., and Clegg, R. M. (1990) Binding characteristics of Hoechst 33258 with calf thymus DNA, poly[d(A-T)] and d(CCGGAATTCCGG): multiple stoichiometries and determination of tight binding with a wide spectrum of site affinities, Biochemistry 29, 9029-9039.
    • (1990) Biochemistry , vol.29 , pp. 9029-9039
    • Loontiens, F.G.1    Regenfuss, P.2    Zechel, A.3    Dumortier, L.4    Clegg, R.M.5
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 37
    • 4043162793 scopus 로고    scopus 로고
    • VEGA-An open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming
    • Pedretti, A., Villa, L., and Vistoli, G. (2004) VEGA-An open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming, J. Comput.-Aided Mol. Des. 18, 167-173.
    • (2004) J. Comput.-Aided Mol. Des. , vol.18 , pp. 167-173
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 39
    • 0037082421 scopus 로고    scopus 로고
    • Complete disproportionation of duplex poly(dT)*poly(dA) into triplex poly(dT)*poly(dA)*poly(dT) and poly(dA) by coralyne
    • Polak, M., and Hud, N. V. (2002) Complete disproportionation of duplex poly(dT)*poly(dA) into triplex poly(dT)*poly(dA)*poly(dT) and poly(dA) by coralyne, Nucleic Acids Res. 30, 983-992.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 983-992
    • Polak, M.1    Hud, N.V.2
  • 40
    • 0020440236 scopus 로고
    • Determination of binding stoichiometry by the continuous variation method: The Job plot
    • Huang, C. Y. (1982) Determination of binding stoichiometry by the continuous variation method: the Job plot, Methods Enzymol. 87, 509-525.
    • (1982) Methods Enzymol. , vol.87 , pp. 509-525
    • Huang, C.Y.1
  • 41
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant, J. M. (1977) Heat capacity and entropy changes in processes involving proteins, Proc. Natl. Acad. Sci. U.S.A. 74, 2236-2240.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 42
    • 0016724739 scopus 로고
    • Optical studies of the interaction of 33258 Hoechst with DNA, chromatin, and metaphase chromosomes
    • Latt, S. A., and Wohlleb, J. C. (1975) Optical studies of the interaction of 33258 Hoechst with DNA, chromatin, and metaphase chromosomes, Chromosoma 52, 297-316.
    • (1975) Chromosoma , vol.52 , pp. 297-316
    • Latt, S.A.1    Wohlleb, J.C.2
  • 43
    • 0038137213 scopus 로고    scopus 로고
    • Ensemble and single-molecule fluorescence spectroscopic study of the binding modes of the bis-benzimidazole derivative Hoechst 33258 with DNA
    • Adhikary, A., Buschmann, V., Muller, C., and Sauer, M. (2003) Ensemble and single-molecule fluorescence spectroscopic study of the binding modes of the bis-benzimidazole derivative Hoechst 33258 with DNA, Nucleic Acids Res. 31, 2178-2186.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2178-2186
    • Adhikary, A.1    Buschmann, V.2    Muller, C.3    Sauer, M.4
  • 44
    • 0019376372 scopus 로고
    • The interaction of intercalating drugs with nucleic acids
    • Berman, H. M., and Young, P. R. (1981) The interaction of intercalating drugs with nucleic acids, Annu. Rev. Biophys. Bioeng. 10, 87-114.
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 87-114
    • Berman, H.M.1    Young, P.R.2
  • 45
    • 0027337134 scopus 로고
    • The different binding modes of Hoechst 33258 to DNA studied by electric linear dichroism
    • (a) Bailly, C., Colson, P., Henichart, J. P., and Houssier, C. (1993) The different binding modes of Hoechst 33258 to DNA studied by electric linear dichroism, Nucleic Acids Res. 21, 3705-3709;
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3705-3709
    • Bailly, C.1    Colson, P.2    Henichart, J.P.3    Houssier, C.4
  • 46
    • 0028858426 scopus 로고
    • Use of electric linear dichroism and competition experiments with intercalating drugs to investigate the mode of binding of Hoechst 33258, berenil and DAPI to GC sequences
    • (b) Colson, P., Houssier, C., and Bailly, C. (1995) Use of electric linear dichroism and competition experiments with intercalating drugs to investigate the mode of binding of Hoechst 33258, berenil and DAPI to GC sequences, J. Biomol. Struct. Dyn. 13, 351-366.
    • (1995) J. Biomol. Struct. Dyn. , vol.13 , pp. 351-366
    • Colson, P.1    Houssier, C.2    Bailly, C.3
  • 47
    • 0002810705 scopus 로고
    • The molecular exciton model
    • (Augenstein, L., Mason, R., and Rosenberg, B., Eds.), Academic Press, New York
    • McRae, E. G., and Kasha, M. L. (1964) The molecular exciton model, in Physical Processes in Radiation Biology (Augenstein, L., Mason, R., and Rosenberg, B., Eds.) pp 23-42, Academic Press, New York.
    • (1964) Physical Processes in Radiation Biology , pp. 23-42
    • McRae, E.G.1    Kasha, M.L.2
  • 48
    • 0033531661 scopus 로고    scopus 로고
    • Spontaneous assembly of helical cyanine dye aggregates on DNA nanotemplates
    • Seifert, J. L., Connor, R. E., Kushon, S. A., Wang, M., and Armitage, B. A. (1999) Spontaneous assembly of helical cyanine dye aggregates on DNA nanotemplates. J. Am. Chem. Soc. 121, 2987-2995.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2987-2995
    • Seifert, J.L.1    Connor, R.E.2    Kushon, S.A.3    Wang, M.4    Armitage, B.A.5
  • 49
    • 0038043319 scopus 로고    scopus 로고
    • Spectroscopic studies of the multiple binding modes of a trimethine-bridged cyanine dye with DNA
    • Sovenyhazy, K. M., Bordelon, J. A., and Petty, J. T. (2003) Spectroscopic studies of the multiple binding modes of a trimethine-bridged cyanine dye with DNA, Nucleic Acids Res. 31, 2561-2569.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2561-2569
    • Sovenyhazy, K.M.1    Bordelon, J.A.2    Petty, J.T.3
  • 50
    • 0037102402 scopus 로고    scopus 로고
    • Determination of affinity, stoichiometry and sequence selectivity of minor groove binder complexes with double-stranded oligodeoxynucleotides by electrospray ionization mass spectrometry
    • Rosu, F., Gabelica, V., Houssier, C., and De Pauw, E. (2002) Determination of affinity, stoichiometry and sequence selectivity of minor groove binder complexes with double-stranded oligodeoxynucleotides by electrospray ionization mass spectrometry, Nucleic Acids Res. 30, e82.
    • (2002) Nucleic Acids Res. , vol.30
    • Rosu, F.1    Gabelica, V.2    Houssier, C.3    De Pauw, E.4
  • 51
    • 0035967528 scopus 로고    scopus 로고
    • Double-stranded DNA binding characteristics and subcellular distribution of a minor groove binding diphenyl ether bisbenzimidazole
    • Satz, A. L., White, C. M., Beerman, T. A., and Bruice, T. C. (2001) Double-stranded DNA binding characteristics and subcellular distribution of a minor groove binding diphenyl ether bisbenzimidazole, Biochemistry 40, 6465-6474.
    • (2001) Biochemistry , vol.40 , pp. 6465-6474
    • Satz, A.L.1    White, C.M.2    Beerman, T.A.3    Bruice, T.C.4
  • 52
    • 4644222022 scopus 로고    scopus 로고
    • Volume errors in isothermal titration calorimetry
    • Tellinghuisen, J. (2004) Volume errors in isothermal titration calorimetry, Anal. Biochem. 333, 405-406.
    • (2004) Anal. Biochem. , vol.333 , pp. 405-406
    • Tellinghuisen, J.1
  • 53
    • 22244467382 scopus 로고    scopus 로고
    • 2: Volumetric, calorimetric, and spectroscopic characterizations
    • 2: volumetric, calorimetric, and spectroscopic characterizations, Biochemistry 44, 9785-9794.
    • (2005) Biochemistry , vol.44 , pp. 9785-9794
    • Han, F.1    Taulier, N.2    Chalikian, T.V.3
  • 54
    • 0034536719 scopus 로고    scopus 로고
    • Thermodynamics of nucleic acids and their interactions with ligands
    • Lane, A. N., and Jenkins, T. C. (2000) Thermodynamics of nucleic acids and their interactions with ligands, Q. Rev. Biophys. 33, 255-306.
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 255-306
    • Lane, A.N.1    Jenkins, T.C.2
  • 55
    • 0037378942 scopus 로고    scopus 로고
    • Energetics of sequence-specific protein-DNA association: Binding of integrase Tn916 to its target DNA
    • Milev, S., Gorfe, A. A., Karshikoff, A., Clubb, R. T., Bosshard, H. R., and Jelesarov, I. (2003) Energetics of sequence-specific protein-DNA association: binding of integrase Tn916 to its target DNA, Biochemistry 42, 3481-3491.
    • (2003) Biochemistry , vol.42 , pp. 3481-3491
    • Milev, S.1    Gorfe, A.A.2    Karshikoff, A.3    Clubb, R.T.4    Bosshard, H.R.5    Jelesarov, I.6
  • 56
    • 0036647051 scopus 로고    scopus 로고
    • Thermodynamics of drug-DNA interactions
    • Haq, I. (2002) Thermodynamics of drug-DNA interactions, Arch. Biochem. Biophys. 403, 1-15.
    • (2002) Arch. Biochem. Biophys. , vol.403 , pp. 1-15
    • Haq, I.1
  • 57
    • 0034713855 scopus 로고    scopus 로고
    • Energetics of DNA intercalation reactions
    • Ren, J. S., Jenkins, T. C., and Chaires, J. B. (2000) Energetics of DNA intercalation reactions, Biochemistry 39, 8439-8447.
    • (2000) Biochemistry , vol.39 , pp. 8439-8447
    • Ren, J.S.1    Jenkins, T.C.2    Chaires, J.B.3
  • 58
    • 0024296533 scopus 로고
    • The molecular structure of the complex of Hoechst 33258 and the DNA dodecamer d(CGCGAATTCGCG)
    • Teng, M., Usman, N., Frederick, C., and Wang, A. (1988) The molecular structure of the complex of Hoechst 33258 and the DNA dodecamer d(CGCGAATTCGCG), Nucleic Acids Res. 16, 2671-2690.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2671-2690
    • Teng, M.1    Usman, N.2    Frederick, C.3    Wang, A.4
  • 60
    • 0029130871 scopus 로고
    • Macromolecules and water: Probing with osmotic stress
    • Parsegian, V. A., Rand, R. P., and Rau, D. C. (1995) Macromolecules and water: probing with osmotic stress, Methods Enzymol. 259, 43-94.
    • (1995) Methods Enzymol. , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 61
    • 0034681955 scopus 로고    scopus 로고
    • Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro
    • Courtenay, E. S., Capp, M. W., Anderson, C. F., and Record, M. T., Jr. (2000) Vapor pressure osmometry studies of osmolyte-protein interactions: implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro, Biochemistry 39, 4455-4471.
    • (2000) Biochemistry , vol.39 , pp. 4455-4471
    • Courtenay, E.S.1    Capp, M.W.2    Anderson, C.F.3    Record Jr., M.T.4
  • 62
    • 8744318698 scopus 로고    scopus 로고
    • Preferential interactions of glycine betaine and of urea with DNA: Implications for DNA hydration and for effects of these solutes on DNA stability
    • Hong, J., Capp, M. W., Anderson, C. F., Saecker, R. M., Felitsky, D. J., Anderson, M. W., and Record, M. T., Jr. (2004) Preferential interactions of glycine betaine and of urea with DNA: implications for DNA hydration and for effects of these solutes on DNA stability, Biochemistry: 43, 14744-14758.
    • (2004) Biochemistry , vol.43 , pp. 14744-14758
    • Hong, J.1    Capp, M.W.2    Anderson, C.F.3    Saecker, R.M.4    Felitsky, D.J.5    Anderson, M.W.6    Record Jr., M.T.7
  • 64
    • 7744221005 scopus 로고    scopus 로고
    • The effect of molecular crowding with nucleotide length and cosolute structure on DNA duplex stability
    • Nakano, S., Karimata, H., Ohmichi, T., Kawakami, J., and Sugimoto, N. (2004) The effect of molecular crowding with nucleotide length and cosolute structure on DNA duplex stability, J. Am. Chem. Soc. 126, 14330-14331.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14330-14331
    • Nakano, S.1    Karimata, H.2    Ohmichi, T.3    Kawakami, J.4    Sugimoto, N.5
  • 67
    • 0019843568 scopus 로고
    • Structure of a B-DNA dodecamer. III. Geometry of hydration
    • Drew, H. R., and Dickerson, R. E. (1981) Structure of a B-DNA dodecamer. III. Geometry of hydration. J. Mol. Biol. 151, 535-556.
    • (1981) J. Mol. Biol. , vol.151 , pp. 535-556
    • Drew, H.R.1    Dickerson, R.E.2
  • 68
    • 0032499635 scopus 로고    scopus 로고
    • The B-DNA dodecamer at high resolution reveals a spine of water on sodium
    • Shui, X., McFail-Isom, L., Hu, G. G., and Williams, L. D. (1998) The B-DNA dodecamer at high resolution reveals a spine of water on sodium, Biochemistry 37, 8341-8355.
    • (1998) Biochemistry , vol.37 , pp. 8341-8355
    • Shui, X.1    McFail-Isom, L.2    Hu, G.G.3    Williams, L.D.4
  • 69
    • 0028931707 scopus 로고
    • The osmotic sensitivity of netropsin analogue binding to DNA
    • Sidorova, N. Y., and Rau, D. C. (1995) The osmotic sensitivity of netropsin analogue binding to DNA, Biopolymers 35, 377-384.
    • (1995) Biopolymers , vol.35 , pp. 377-384
    • Sidorova, N.Y.1    Rau, D.C.2
  • 70
    • 0035835086 scopus 로고    scopus 로고
    • Hydration changes for DNA intercalation reactions
    • Qu, X., and Chaires, J. B. (2001) Hydration changes for DNA intercalation reactions, J. Am. Chem. Soc. 123, 1-7.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1-7
    • Qu, X.1    Chaires, J.B.2
  • 71
    • 0031875837 scopus 로고    scopus 로고
    • Effects of pressure on the DNA minor groove binding of Hoechst 33258
    • Tang, G. Q., Tanaka, N., and Kunugi, S. (1998) Effects of pressure on the DNA minor groove binding of Hoechst 33258, Bull. Chem. Soc. Jpn. 71, 1725-1730.
    • (1998) Bull. Chem. Soc. Jpn. , vol.71 , pp. 1725-1730
    • Tang, G.Q.1    Tanaka, N.2    Kunugi, S.3
  • 72
    • 0032788299 scopus 로고    scopus 로고
    • 2 complex determined by NMR and molecular dynamics simulations in solution
    • 2 complex determined by NMR and molecular dynamics simulations in solution, J. Mol. Biol. 290, 699-716.
    • (1999) J. Mol. Biol. , vol.290 , pp. 699-716
    • Williams, H.E.L.1    Searle, M.S.2
  • 73
    • 0029144073 scopus 로고
    • Hydrostatic and osmotic pressure as tools to study macromolecular recognition
    • Robinson, C. R., and Sugar, S. G. (1995) Hydrostatic and osmotic pressure as tools to study macromolecular recognition, Methods Enzymol. (Energ. Biol. Macromol.) 259, 395-427.
    • (1995) Methods Enzymol. (Energ. Biol. Macromol.) , vol.259 , pp. 395-427
    • Robinson, C.R.1    Sugar, S.G.2
  • 74
    • 0842342617 scopus 로고    scopus 로고
    • Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments
    • Shimizu, S. (2004) Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments. Proc. Natl. Acad. Sci. U.S.A. 101, 1195-1199.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1195-1199
    • Shimizu, S.1
  • 75
    • 0025272657 scopus 로고
    • Crystal structure of a berenil-dodecanucleotide complex: The role of water in sequence-specific ligand binding
    • Brown, D., Sanderson, M., Skelly, J., Jenkins, T., Brown, T., Garman, E., Stuart, D., and Neidle, S. (1990) Crystal structure of a berenil- dodecanucleotide complex: the role of water in sequence-specific ligand binding, EMBO J. 9, 1329-1334.
    • (1990) EMBO J. , vol.9 , pp. 1329-1334
    • Brown, D.1    Sanderson, M.2    Skelly, J.3    Jenkins, T.4    Brown, T.5    Garman, E.6    Stuart, D.7    Neidle, S.8
  • 76
    • 0037337378 scopus 로고    scopus 로고
    • Sequence-specific minor groove binding by bis-benzimidazoles: Water molecules in ligand recognition
    • Bailly, C., Chessari, G., Carrasco, C., Joubert, A., Mann, J., Wilson, W. D., and Neidle, S. (2003) Sequence-specific minor groove binding by bis-benzimidazoles: water molecules in ligand recognition, Nucleic Acids Res. 31, 1514-1524.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1514-1524
    • Bailly, C.1    Chessari, G.2    Carrasco, C.3    Joubert, A.4    Mann, J.5    Wilson, W.D.6    Neidle, S.7
  • 78
    • 0027772178 scopus 로고
    • Crystal-structure of d(CGCGAATTCGCG) complexed with propamidine, a short-chain homologue of the drug pentamidine
    • Nunn, C. M., Jenkins, T. C., and Neidle, S. (1993) Crystal-structure of d(CGCGAATTCGCG) complexed with propamidine, a short-chain homologue of the drug pentamidine, Biochemistry 32, 13838-13843.
    • (1993) Biochemistry , vol.32 , pp. 13838-13843
    • Nunn, C.M.1    Jenkins, T.C.2    Neidle, S.3
  • 79
    • 0026896780 scopus 로고
    • Hydration of DNA bases: Analysis of crystallographic data
    • Schneider, B., Cohen, D., and Berman, H. M. (1992) Hydration of DNA bases: analysis of crystallographic data, Biopolymers 32, 725-750.
    • (1992) Biopolymers , vol.32 , pp. 725-750
    • Schneider, B.1    Cohen, D.2    Berman, H.M.3
  • 83
    • 0037816372 scopus 로고    scopus 로고
    • Water at DNA surfaces: Ultrafast dynamics in minor groove recognition
    • Pal, S. K., Zhao, L., and Zewail, A. H. (2003) Water at DNA surfaces: Ultrafast dynamics in minor groove recognition, Proc. Natl. Acad. Sci. U.S.A. 100, 8113-8118.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8113-8118
    • Pal, S.K.1    Zhao, L.2    Zewail, A.H.3
  • 85
    • 0025109561 scopus 로고
    • Minor-groove recognition of the self-complementary duplex d(CGCGAATTCGCG)2 by Hoechst 33258: A high-field NMR study
    • Parkinson, J. A., Barber, J., Douglas, K. T., Rosamond, J., and Sharples, D. (1990) Minor-groove recognition of the self-complementary duplex d(CGCGAATTCGCG)2 by Hoechst 33258: a high-field NMR study, Biochemistry 29, 10181-10190.
    • (1990) Biochemistry , vol.29 , pp. 10181-10190
    • Parkinson, J.A.1    Barber, J.2    Douglas, K.T.3    Rosamond, J.4    Sharples, D.5
  • 88
    • 0024974059 scopus 로고
    • Binding of a Hoechst dye to d(CGCGATATCGCG) and its influence on the conformation of the DNA fragment
    • Carrondo, M. A., Coll, M., Aymami, J., Wang, A. H., van der Marel, G. A., van Boom, J. H., and Rich, A. (1989) Binding of a Hoechst dye to d(CGCGATATCGCG) and its influence on the conformation of the DNA fragment, Biochemistry 28, 7849-7859.
    • (1989) Biochemistry , vol.28 , pp. 7849-7859
    • Carrondo, M.A.1    Coll, M.2    Aymami, J.3    Wang, A.H.4    Van Der Marel, G.A.5    Van Boom, J.H.6    Rich, A.7


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