메뉴 건너뛰기




Volumn 268, Issue 1, 1997, Pages 118-136

Kinetics of DNA hydration

Author keywords

B DNA hydration; Netropsin; NMR spectroscopy; Oxygen 17 relaxation dispersion; Water residence time

Indexed keywords

CONGOCIDINE; DEUTERIUM; DNA B; DOUBLE STRANDED DNA; OXYGEN; PROTON; WATER;

EID: 0031585991     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0862     Document Type: Article
Times cited : (127)

References (91)
  • 2
    • 0002335699 scopus 로고
    • Solvent interactions with proteins as revealed by X-ray crystallographic studies
    • New York: M. Dekker
    • Baker E. N. Solvent interactions with proteins as revealed by X-ray crystallographic studies. Protein-Solvent Interactions. 1995;M. Dekker, New York.
    • (1995) Protein-Solvent Interactions
    • Baker, E.N.1
  • 6
    • 36149018202 scopus 로고
    • Radiation damping in magnetic resonance experiments
    • Bloembergen N., Pound R. V. Radiation damping in magnetic resonance experiments. Phys. Rev. 95:1954;8-12.
    • (1954) Phys. Rev. , vol.95 , pp. 8-12
    • Bloembergen, N.1    Pound, R.V.2
  • 9
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By A. A., Stephens R. L., Lee J., Warren C. D., Jeanloz R. W. Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc. 106:1984;811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.3    Warren, C.D.4    Jeanloz, R.W.5
  • 10
    • 0002368263 scopus 로고
    • Water self-diffusion model for protein-water NMR cross relaxation
    • Brüschweiler R., Wright P. E. Water self-diffusion model for protein-water NMR cross relaxation. Chem. Phys. Letters. 229:1994;75-81.
    • (1994) Chem. Phys. Letters , vol.229 , pp. 75-81
    • Brüschweiler, R.1    Wright, P.E.2
  • 11
    • 0011170214 scopus 로고
    • Water dynamics in microemulsion droplets. A nuclear spin relaxation study
    • Carlström G., Halle B. Water dynamics in microemulsion droplets. A nuclear spin relaxation study. Langmuir. 4:1988;1346-1352.
    • (1988) Langmuir , vol.4 , pp. 1346-1352
    • Carlström, G.1    Halle, B.2
  • 12
    • 0028142863 scopus 로고
    • Influence of drug binding on DNA hydration: Acoustic and densimetric characterizations of netropsin binding to the poly(dAdT)·poly(dAdT) and poly(dA)·poly(dT) duplexes and the poly(dT)·poly(dA)·poly(dT) triplex at 25°C
    • Chalikian T. V., Plum G. E., Sarvazyan A. P., Breslauer K. J. Influence of drug binding on DNA hydration: acoustic and densimetric characterizations of netropsin binding to the poly(dAdT)·poly(dAdT) and poly(dA)·poly(dT) duplexes and the poly(dT)·poly(dA)·poly(dT) triplex at 25°C. Biochemistry. 33:1994;8629-8640.
    • (1994) Biochemistry , vol.33 , pp. 8629-8640
    • Chalikian, T.V.1    Plum, G.E.2    Sarvazyan, A.P.3    Breslauer, K.J.4
  • 13
    • 0029170114 scopus 로고
    • Molecular dynamics simulations on solvated biomolecular systems: The particle mesh Evald method leads to stable trajectories of DNA, RNA, and proteis
    • Cheatham T. E., Miller J. L., Fox T., Darden T. A., Kollman P. A. Molecular dynamics simulations on solvated biomolecular systems: the particle mesh Evald method leads to stable trajectories of DNA, RNA, and proteis. J. Am. Chem. Soc. 117:1995;4193-4194.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 4193-4194
    • Cheatham, T.E.1    Miller, J.L.2    Fox, T.3    Darden, T.A.4    Kollman, P.A.5
  • 14
    • 0026019603 scopus 로고
    • Molecular dynamics simulation of the hydration shell of a B -DNA decamer revals two main types of minor-groove hydration depending on groove width
    • Chuprina V. P., Heinemann U., Nurislamov A. A., Zielenbkiewicz P., Dickerson R. E., Saenger W. Molecular dynamics simulation of the hydration shell of a B -DNA decamer revals two main types of minor-groove hydration depending on groove width. Proc. Natl Acad. Sci. USA. 88:1991;593-597.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 593-597
    • Chuprina, V.P.1    Heinemann, U.2    Nurislamov, A.A.3    Zielenbkiewicz, P.4    Dickerson, R.E.5    Saenger, W.6
  • 15
    • 0028773080 scopus 로고
    • Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA
    • Clore G. M., Bax A., Omichinski J. G., Gronenborn A. M. Localization of bound water in the solution structure of a complex of the erythroid transcription factor GATA-1 with DNA. Structure. 1:1994;89-94.
    • (1994) Structure , vol.1 , pp. 89-94
    • Clore, G.M.1    Bax, A.2    Omichinski, J.G.3    Gronenborn, A.M.4
  • 16
    • 0028948786 scopus 로고
    • Protein hydration dynamics in aqueous solution: A comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion
    • Denisov V. P., Halle B. Protein hydration dynamics in aqueous solution: a comparison of bovine pancreatic trypsin inhibitor and ubiquitin by oxygen-17 spin relaxation dispersion. J. Mol. Biol. 245:1995a;682-697.
    • (1995) J. Mol. Biol. , vol.245 , pp. 682-697
    • Denisov, V.P.1    Halle, B.2
  • 17
    • 0028937274 scopus 로고
    • Hydrogen exchange and protein hydration: The deuteron spin relaxation dispersions of bovine pancreatic trypsin inhibitor and ubiquitin
    • Denisov V. P., Halle B. Hydrogen exchange and protein hydration: the deuteron spin relaxation dispersions of bovine pancreatic trypsin inhibitor and ubiquitin. J. Mol. Biol. 245:1995b;698-709.
    • (1995) J. Mol. Biol. , vol.245 , pp. 698-709
    • Denisov, V.P.1    Halle, B.2
  • 18
    • 0028871018 scopus 로고
    • 9kby nuclear magnetic relaxation dispersion
    • 9kby nuclear magnetic relaxation dispersion. J. Am. Chem. Soc. 117:1995c;8456-8465.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8456-8465
    • Denisov, V.P.1    Halle, B.2
  • 19
    • 0030325741 scopus 로고    scopus 로고
    • Protein hydration dynamics in aqueous solution
    • in the press
    • Denisov V. P., Halle B. Protein hydration dynamics in aqueous solution. Faraday Discuss. 103:1996;in the press.
    • (1996) Faraday Discuss , vol.103
    • Denisov, V.P.1    Halle, B.2
  • 20
    • 0029081424 scopus 로고
    • Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant
    • Denisov V. P., Halle B., Peters J., Hörlein H. D. Residence times of the buried water molecules in bovine pancreatic trypsin inhibitor and its G36S mutant. Biochemistry. 34:1995;9046-9051.
    • (1995) Biochemistry , vol.34 , pp. 9046-9051
    • Denisov, V.P.1    Halle, B.2    Peters, J.3    Hörlein, H.D.4
  • 21
    • 0029994817 scopus 로고    scopus 로고
    • Using buried water molecules to explore the energy landscape of proteins
    • Denisov V. P., Peters J., Hörlein H. D., Halle B. Using buried water molecules to explore the energy landscape of proteins. Nature Struct. Biol. 3:1996;505-509.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 505-509
    • Denisov, V.P.1    Peters, J.2    Hörlein, H.D.3    Halle, B.4
  • 22
    • 0019843568 scopus 로고
    • Structure of a B -DNA dodecamer. III. Geometry of hydration
    • Drew H. R., Dickerson R. E. Structure of a B -DNA dodecamer. III. Geometry of hydration. J. Mol. Biol. 151:1981;535-556.
    • (1981) J. Mol. Biol. , vol.151 , pp. 535-556
    • Drew, H.R.1    Dickerson, R.E.2
  • 23
    • 0029024850 scopus 로고
    • Hydration patterns and intermolecular interactions in A -DNA crystal structures. Implications for DNA recognition
    • Eisenstein M., Shakked Z. Hydration patterns and intermolecular interactions in A -DNA crystal structures. Implications for DNA recognition. J. Mol. Biol. 248:1995;662-678.
    • (1995) J. Mol. Biol. , vol.248 , pp. 662-678
    • Eisenstein, M.1    Shakked, Z.2
  • 24
    • 0000877546 scopus 로고
    • Sequence dependent hydration of DNA: Theoretical results
    • Elcock A. H., McCammon J. A. Sequence dependent hydration of DNA: theoretical results. J. Am. Chem. Soc. 117:1995;10161-10162.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10161-10162
    • Elcock, A.H.1    McCammon, J.A.2
  • 26
    • 0027494366 scopus 로고
    • Structural and dynamic studies of a non-self-complementary dodecamer DNA duplex
    • Fawthrop S. A., Yang J.-C., Fisher J. Structural and dynamic studies of a non-self-complementary dodecamer DNA duplex. Nucl. Acid Res. 21:1993;4860-4866.
    • (1993) Nucl. Acid Res. , vol.21 , pp. 4860-4866
    • Fawthrop, S.A.1    Yang, J.-C.2    Fisher, J.3
  • 27
    • 0000857592 scopus 로고
    • The structure of sodium thymonucleate fibers. I. The influence of water content
    • Franklin R. E., Gosling R. G. The structure of sodium thymonucleate fibers. I. The influence of water content. Acta Crystallog. 6:1953;673-677.
    • (1953) Acta Crystallog. , vol.6 , pp. 673-677
    • Franklin, R.E.1    Gosling, R.G.2
  • 28
    • 0028956354 scopus 로고
    • Refinement of netropsin bound to DNA: Bias and feedback in electron density map interpretation
    • Goodsell D. S., Kopka M. L., Dickerson R. E. Refinement of netropsin bound to DNA: bias and feedback in electron density map interpretation. Biochemistry. 34:1995;4983-4993.
    • (1995) Biochemistry , vol.34 , pp. 4983-4993
    • Goodsell, D.S.1    Kopka, M.L.2    Dickerson, R.E.3
  • 29
    • 0028945546 scopus 로고
    • Absorption and circular dichroism spectroscopy of nucleic acid duplexes and triplexes
    • Gray D. M., Hung S.-H., Johnson K. H. Absorption and circular dichroism spectroscopy of nucleic acid duplexes and triplexes. Methods Enzymol. 246:1995;19-34.
    • (1995) Methods Enzymol. , vol.246 , pp. 19-34
    • Gray, D.M.1    Hung, S.-H.2    Johnson, K.H.3
  • 30
    • 0001240703 scopus 로고
    • Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy
    • Griesinger C., Ernst R. R. Frequency offset effects and their elimination in NMR rotating-frame cross-relaxation spectroscopy. J. Magn. Reson. 75:1987;261-271.
    • (1987) J. Magn. Reson. , vol.75 , pp. 261-271
    • Griesinger, C.1    Ernst, R.R.2
  • 31
    • 0028864424 scopus 로고
    • Studies of base pair kinetics by NMR measurement of proton exchange
    • Guéron M., Leroy J.-L. Studies of base pair kinetics by NMR measurement of proton exchange. Methods Enzymol. 261:1995;383-413.
    • (1995) Methods Enzymol. , vol.261 , pp. 383-413
    • Guéron, M.1    Leroy, J.-L.2
  • 32
    • 37049106425 scopus 로고
    • Prototropic charge migration in water. Rate constants in light and heavy water and in salt solution from oxygen-17 spin relaxation
    • Halle B., Karlström G. Prototropic charge migration in water. Rate constants in light and heavy water and in salt solution from oxygen-17 spin relaxation. J. Chem. Soc., Faraday Trans. 2. 79:1983;1031-1046.
    • (1983) J. Chem. Soc., Faraday Trans. 2 , vol.79 , pp. 1031-1046
    • Halle, B.1    Karlström, G.2
  • 33
    • 2942697858 scopus 로고
    • Interpretation of magnetic resonance data from water nuclei in heterogeneous systems
    • Halle B., Wennerström H. Interpretation of magnetic resonance data from water nuclei in heterogeneous systems. J. Chem. Phys. 75:1981;1928-1943.
    • (1981) J. Chem. Phys. , vol.75 , pp. 1928-1943
    • Halle, B.1    Wennerström, H.2
  • 34
    • 0020484560 scopus 로고
    • 6A-U from proton NMR chemical shifts: Differential concentration temperature profile method
    • 6A-U from proton NMR chemical shifts: differential concentration temperature profile method. Eur. J. Biochem. 129:1982;343-357.
    • (1982) Eur. J. Biochem. , vol.129 , pp. 343-357
    • Hartel, A.J.1    Lankhorst, P.P.2    Altona, C.3
  • 36
    • 0000984545 scopus 로고
    • A proton magnetic resonance study of the hydration of deoxyribonucleic acid
    • Jacobson B., Anderson W. A., Arnold J. T. A proton magnetic resonance study of the hydration of deoxyribonucleic acid. Nature. 173:1954;772-773.
    • (1954) Nature , vol.173 , pp. 772-773
    • Jacobson, B.1    Anderson, W.A.2    Arnold, J.T.3
  • 38
    • 0029157054 scopus 로고
    • Hydration and solution structure of nucleic acids
    • Kochoyan M., Leroy J. L. Hydration and solution structure of nucleic acids. Curr. Opin. Struct. Biol. 5:1995;329-333.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 329-333
    • Kochoyan, M.1    Leroy, J.L.2
  • 39
    • 0020692923 scopus 로고
    • Ordered water structure around a B -DNA dodecamer. A quantitative study
    • Kopka M. L., Fratini A. V., Drew H. R., Dickerson R. E. Ordered water structure around a B -DNA dodecamer. A quantitative study. J. Mol. Biol. 163:1983;129-146.
    • (1983) J. Mol. Biol. , vol.163 , pp. 129-146
    • Kopka, M.L.1    Fratini, A.V.2    Drew, H.R.3    Dickerson, R.E.4
  • 42
    • 0000235752 scopus 로고
    • NMR evidence for DNA bound water in solution
    • Kubinec M. G., Wemmer D. E. NMR evidence for DNA bound water in solution. J. Am. Chem. Soc. 114:1992;8739-8740.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8739-8740
    • Kubinec, M.G.1    Wemmer, D.E.2
  • 43
    • 0030051552 scopus 로고    scopus 로고
    • Proton exchange rates from amino acid side chains-implications for image contrast
    • Liepinsh E., Otting G. Proton exchange rates from amino acid side chains-implications for image contrast. Magn. Reson. Med. 35:1996;30-42.
    • (1996) Magn. Reson. Med. , vol.35 , pp. 30-42
    • Liepinsh, E.1    Otting, G.2
  • 44
    • 0027058824 scopus 로고
    • NMR observation of individual molecules of hydration water bound to DNA duplexes: Direct evidence for a spine of hydration water present in aqueous solution
    • Liepinsh E., Otting G., Wüthrich K. NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution. Nucl. Acid Res. 20:1992;6549-6553.
    • (1992) Nucl. Acid Res. , vol.20 , pp. 6549-6553
    • Liepinsh, E.1    Otting, G.2    Wüthrich, K.3
  • 46
    • 0027403859 scopus 로고
    • Structure of the B -DNA decamer CCAACITTGG in two different space groups: Conformational flexibility of B -DNA
    • Lipanov A., Kopka M. L., Kaczor-Grzeskowiak M., Quintana J., Dickerson R. E. Structure of the B -DNA decamer CCAACITTGG in two different space groups: conformational flexibility of B -DNA. Biochemisty. 32:1993;1373-1380.
    • (1993) Biochemisty , vol.32 , pp. 1373-1380
    • Lipanov, A.1    Kopka, M.L.2    Kaczor-Grzeskowiak, M.3    Quintana, J.4    Dickerson, R.E.5
  • 47
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:1982;4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 48
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura S., Ernst R. R. Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41:1980;95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • MacUra, S.1    Ernst, R.R.2
  • 49
    • 0027317074 scopus 로고
    • How much hydration is necessary for the stabilisation of DNA-duplex?
    • Maltseva T. V., Agback P., Chattopadhyaya J. How much hydration is necessary for the stabilisation of DNA-duplex? Nucl. Acids Res. 21:1993;4246-4252.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 4246-4252
    • Maltseva, T.V.1    Agback, P.2    Chattopadhyaya, J.3
  • 50
    • 0000201496 scopus 로고
    • Radiation damping effects on spin-lattice relaxation time measurements
    • Mao X., Guo J., Ye C. Radiation damping effects on spin-lattice relaxation time measurements. Chem. Phys. Letters. 222:1994;417-421.
    • (1994) Chem. Phys. Letters , vol.222 , pp. 417-421
    • Mao, X.1    Guo, J.2    Ye, C.3
  • 51
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D., Ikura M., Tschudin R., Bax A. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85:1989;393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 52
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • Marky L. A., Breslauer K. J. Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers. 26:1987;1601-1620.
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Breslauer, K.J.2
  • 53
    • 0020579962 scopus 로고
    • Salt-dependent conformational transitions in the self-complementary deoxydodecanucleotide d(CGCGAATTCGCG): Evidence for hairpin formation
    • Marky L. A., Blumenfeld K. S., Kozlowski S., Breslauer K. J. Salt-dependent conformational transitions in the self-complementary deoxydodecanucleotide d(CGCGAATTCGCG): evidence for hairpin formation. Biopolymers. 22:1983;1247-1257.
    • (1983) Biopolymers , vol.22 , pp. 1247-1257
    • Marky, L.A.1    Blumenfeld, K.S.2    Kozlowski, S.3    Breslauer, K.J.4
  • 54
    • 0025787463 scopus 로고
    • Crystal and molecular structure of a DNA fragment: D(CGTGAATTCACG)
    • Narayana N., Ginell S. L., Russu I., Berman H. M. Crystal and molecular structure of a DNA fragment: d(CGTGAATTCACG). Biochemistry. 30:1991;4449-4455.
    • (1991) Biochemistry , vol.30 , pp. 4449-4455
    • Narayana, N.1    Ginell, S.L.2    Russu, I.3    Berman, H.M.4
  • 55
    • 0024788819 scopus 로고
    • Solution structure of the Eco RI DNA sequence: Refinement of NMR-derived distance geometry structures by NOESY specrum back-calculations
    • Nerdal W., Hare D. R., Reid B. R. Solution structure of the Eco RI DNA sequence: refinement of NMR-derived distance geometry structures by NOESY specrum back-calculations. Biochemistry. 28:1989;10008-10021.
    • (1989) Biochemistry , vol.28 , pp. 10008-10021
    • Nerdal, W.1    Hare, D.R.2    Reid, B.R.3
  • 56
    • 0026319199 scopus 로고
    • Protein folding and association. Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association. Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 59
    • 0000547870 scopus 로고
    • Protein hydration viewed by high-resolution NMR spectroscopy: Implications for magnetic resonance image contrast
    • Otting G., Liepinsh E. Protein hydration viewed by high-resolution NMR spectroscopy: implications for magnetic resonance image contrast. Acc. Chem. Res. 28:1995;171-177.
    • (1995) Acc. Chem. Res. , vol.28 , pp. 171-177
    • Otting, G.1    Liepinsh, E.2
  • 60
    • 0000857486 scopus 로고
    • Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules
    • Otting G., Wüthrich K. Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. J. Am. Chem. Soc. 111:1989;1871-1875.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1871-1875
    • Otting, G.1    Wüthrich, K.2
  • 62
    • 0026326956 scopus 로고
    • Protein hydration in aqueous solution
    • Otting G., Liepinsh E., Wüthrich K. Protein hydration in aqueous solution. Science. 254:1991b;974-980.
    • (1991) Science , vol.254 , pp. 974-980
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 63
    • 0026699126 scopus 로고
    • Polypeptide hydration in mixed solvents at low temperatures
    • Otting G., Liepinsh E., Wüthrich K. Polypeptide hydration in mixed solvents at low temperatures. J. Am. Chem. Soc. 114:1992;7093-7095.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7093-7095
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 65
    • 0020394591 scopus 로고
    • Antibiotic-DNA interactions: Intermolecular nuclear Overhauser effects in the netropsin-d(CGCGAATTCGCG) complex in solution
    • Patel D. J. Antibiotic-DNA interactions: Intermolecular nuclear Overhauser effects in the netropsin-d(CGCGAATTCGCG) complex in solution. Proc. Natl Acad. Sci. USA. 79:1982;6424-6428.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 6424-6428
    • Patel, D.J.1
  • 68
    • 0000764227 scopus 로고
    • NMR detection of hydration water in the intermolecular interface of a protein-DNA complex
    • Qian Y. Q., Otting G., Wüthrich K. NMR detection of hydration water in the intermolecular interface of a protein-DNA complex. J. Am. Chem. Soc. 115:1993;1189-1190.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 1189-1190
    • Qian, Y.Q.1    Otting, G.2    Wüthrich, K.3
  • 70
    • 0001417283 scopus 로고
    • Netropsin biding as a thermodynamic probe of the grooves of parallel DNA
    • Rentzeperis D., Marky L. A. Netropsin biding as a thermodynamic probe of the grooves of parallel DNA. J. Am. Chem. Soc. 155:1993;1645-1650.
    • (1993) J. Am. Chem. Soc. , vol.155 , pp. 1645-1650
    • Rentzeperis, D.1    Marky, L.A.2
  • 71
    • 0028818563 scopus 로고
    • Site-specific dynamics in DNA: Theory and experiment
    • Robinson B. H., Drobny G. P. Site-specific dynamics in DNA: theory and experiment. Methods Enzymol. 261:1995;451-509.
    • (1995) Methods Enzymol. , vol.261 , pp. 451-509
    • Robinson, B.H.1    Drobny, G.P.2
  • 72
    • 0027372486 scopus 로고
    • Molecular recognition mediated by bound water. A mechanism for star activity of the restriction endonuclease Eco RI
    • Robinson C. R., Sligar S. G. Molecular recognition mediated by bound water. A mechanism for star activity of the restriction endonuclease Eco RI. J. Mol. Biol. 234:1993;302-306.
    • (1993) J. Mol. Biol. , vol.234 , pp. 302-306
    • Robinson, C.R.1    Sligar, S.G.2
  • 73
    • 0023061930 scopus 로고
    • Structure and dynamics of water surrounding biomolecules
    • Saenger W. Structure and dynamics of water surrounding biomolecules. Annu. Rev. Biophys. Biophys. Chem. 16:1987;93-114.
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 93-114
    • Saenger, W.1
  • 74
    • 0028823008 scopus 로고
    • Hydration of the DNA bases is local
    • Schneider B., Berman H. M. Hydration of the DNA bases is local. Biophys. J. 69:1995;2661-2669.
    • (1995) Biophys. J. , vol.69 , pp. 2661-2669
    • Schneider, B.1    Berman, H.M.2
  • 75
  • 76
    • 58149363306 scopus 로고
    • Suppression of radiation damping in multidimensional NMR experiments using magnetic field gradients
    • Sklenar V. Suppression of radiation damping in multidimensional NMR experiments using magnetic field gradients. J. Magn. Reson. ser. A. 114:1995;132-135.
    • (1995) J. Magn. Reson. Ser. a , vol.114 , pp. 132-135
    • Sklenar, V.1
  • 78
    • 0004084360 scopus 로고
    • Light scattering spectroscopy studies of the water molecules in DNA
    • E. Westhof. Boca Raton: CRC Press
    • Tao N. J. Light scattering spectroscopy studies of the water molecules in DNA. Westhof E. Water and Biological Macromolecules. 1993;CRC Press, Boca Raton.
    • (1993) Water and Biological Macromolecules
    • Tao, N.J.1
  • 79
    • 0023284697 scopus 로고
    • The dynamics of the DNA hydration shell at gigahertz frequencies
    • Tao N. J., Lindsay S. M., Rupprecht A. The dynamics of the DNA hydration shell at gigahertz frequencies. Bipolymers. 26:1987;171-188.
    • (1987) Bipolymers , vol.26 , pp. 171-188
    • Tao, N.J.1    Lindsay, S.M.2    Rupprecht, A.3
  • 80
    • 26544473673 scopus 로고
    • Rotational dynamics of rigid, symmetric top macromolecules. Application to circular cylinders
    • Tirado M. M., Garcia de la Torre J. Rotational dynamics of rigid, symmetric top macromolecules. Application to circular cylinders. J. Chem. Phys. 73:1980;1986-1993.
    • (1980) J. Chem. Phys. , vol.73 , pp. 1986-1993
    • Tirado, M.M.1    Garcia De La Torre, J.2
  • 81
    • 0001653652 scopus 로고
    • Chemically relayed nuclear Overhauser effects. Connectivities between resonances of nonexchangeable protons and water
    • van de Ven F. J. M., Janssen H. G. J. M., Gräslund A., Hilbers C. W. Chemically relayed nuclear Overhauser effects. Connectivities between resonances of nonexchangeable protons and water. J. Magn. Reson. 79:1988;221-235.
    • (1988) J. Magn. Reson. , vol.79 , pp. 221-235
    • Van De Ven, F.J.M.1    Janssen, H.G.J.M.2    Gräslund, A.3    Hilbers, C.W.4
  • 82
    • 0030919951 scopus 로고    scopus 로고
    • 1H magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation
    • 1H magnetic relaxation dispersion in protein solutions. A quantitative assessment of internal hydration, proton exchange, and cross-relaxation. J. Am. Chem. Soc.In the press. 1997.
    • (1997) J. Am. Chem. Soc.In the Press
    • Venu, K.1    Denisov, V.P.2    Halle, B.3
  • 84
    • 0023459640 scopus 로고
    • Re-refinement of the B -dodecamer d(CGCGAATTCGCG) with a comparative analysis of the solvent structure in it and in the Z-hexamer d(5BrCG5BrCG5BrCG)
    • Westhof E. Re-refinement of the B -dodecamer d(CGCGAATTCGCG) with a comparative analysis of the solvent structure in it and in the Z-hexamer d(5BrCG5BrCG5BrCG). J. Biomol. Struct. Dynam. 5:1987;581-600.
    • (1987) J. Biomol. Struct. Dynam. , vol.5 , pp. 581-600
    • Westhof, E.1
  • 85
    • 0023708040 scopus 로고
    • Water: An integral part of nucleic acid structure
    • Westhof E. Water: An integral part of nucleic acid structure. Annu. Rev. Biophys. Biophys. Cehm. 17:1988;125-144.
    • (1988) Annu. Rev. Biophys. Biophys. Cehm. , vol.17 , pp. 125-144
    • Westhof, E.1
  • 86
    • 0000514393 scopus 로고
    • Structural water bridges in nucleic acids
    • E. Westhof. Boca Raton: CRC Press
    • Westhof E. Structural water bridges in nucleic acids. Westhof E. Water and Biological Macromolecules. 1993;CRC Press, Boca Raton.
    • (1993) Water and Biological Macromolecules
    • Westhof, E.1
  • 87
    • 0001123057 scopus 로고
    • NMR of nucleic acids; From spectrum to structure
    • G.C.K. Roberts. Oxford: IRL Press
    • Wijmenga S. S., Mooren M. M. W., Hilbers C. W. NMR of nucleic acids; from spectrum to structure. Roberts G. C. K. NMR of Macromolecules. 1993;IRL Press, Oxford.
    • (1993) NMR of Macromolecules
    • Wijmenga, S.S.1    Mooren, M.M.W.2    Hilbers, C.W.3
  • 88
    • 0001495085 scopus 로고
    • Time dependence of nuclear Overhauser effects of duplex DNA from molecular dynamics trajectories
    • Withka J. M., Swaminathan S., Beveridge D. L., Bolton P. H. Time dependence of nuclear Overhauser effects of duplex DNA from molecular dynamics trajectories. J. Am. Chem. Soc. 113:1991;5041-5049.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5041-5049
    • Withka, J.M.1    Swaminathan, S.2    Beveridge, D.L.3    Bolton, P.H.4
  • 89
    • 33644625296 scopus 로고
    • Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion
    • Woessner D. E. Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion. J. Chem. Phys. 37:1962;647-654.
    • (1962) J. Chem. Phys. , vol.37 , pp. 647-654
    • Woessner, D.E.1
  • 90
    • 0029110156 scopus 로고
    • Toward the accurate modeling of DNA: The importance of long-range electrostatics
    • York D. M., Yang W., Lee H., Darden T., Pedersen L. G. Toward the accurate modeling of DNA: the importance of long-range electrostatics. J. Am. Chem. Soc. 117:1995;5001-5002.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5001-5002
    • York, D.M.1    Yang, W.2    Lee, H.3    Darden, T.4    Pedersen, L.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.