메뉴 건너뛰기




Volumn 276, Issue 3, 1998, Pages 571-590

Thermodynamics of specific and non-specific DNA binding by the c-Myb DNA-binding domain

Author keywords

c Myb; DNA binding; Isothermal titration calorimetry; Protein engineering; Thermodynamics

Indexed keywords

DNA BINDING PROTEIN; MUTANT PROTEIN; ONCOPROTEIN; PROTEIN C MYB; UNCLASSIFIED DRUG;

EID: 0032570633     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1564     Document Type: Article
Times cited : (100)

References (72)
  • 1
    • 0018791943 scopus 로고
    • Solvent-accessible surfaces of nucleic acids
    • Alden C. J., Kim S.-H. Solvent-accessible surfaces of nucleic acids. J. Mol. Biol. 132:1979;411-434.
    • (1979) J. Mol. Biol. , vol.132 , pp. 411-434
    • Alden, C.J.1    Kim, S.-H.2
  • 3
    • 0023737377 scopus 로고
    • Viral myb oncogene encodes a sequence-specific DNA-binding activity
    • Biedenkapp H., Borgmeyer U., Sippel A. E., Klempnauer K.-H. Viral myb oncogene encodes a sequence-specific DNA-binding activity. Nature. 335:1988;835-837.
    • (1988) Nature , vol.335 , pp. 835-837
    • Biedenkapp, H.1    Borgmeyer, U.2    Sippel, A.E.3    Klempnauer, K.-H.4
  • 4
    • 0020385863 scopus 로고
    • Mechanics of sequence-dependent stacking of bases in B-DNA
    • Calladine C. R. Mechanics of sequence-dependent stacking of bases in B-DNA. J. Mol. Biol. 161:1982;343-352.
    • (1982) J. Mol. Biol. , vol.161 , pp. 343-352
    • Calladine, C.R.1
  • 5
    • 0027327521 scopus 로고
    • A role in DNA binding for the linker sequences of the first three zinc fingers of TFIIIA
    • Choo Y., Klug A. A role in DNA binding for the linker sequences of the first three zinc fingers of TFIIIA. Nucl. Acids Res. 21:1993;3341-3346.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 3341-3346
    • Choo, Y.1    Klug, A.2
  • 6
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz J. D. The entropic cost of bound water in crystals and biomolecules. Science. 264:1994;670.
    • (1994) Science , vol.264 , pp. 670
    • Dunitz, J.D.1
  • 7
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz J. D. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2:1995;709-712.
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 8
    • 0017869404 scopus 로고
    • Water and proteins. I. The significance and structure of water; Its interaction with electrolytes and non-electrolytes
    • Edsall J. T., McKenzie H. A. Water and proteins. I. The significance and structure of water; its interaction with electrolytes and non-electrolytes. Advan. Biophys. 10:1978;137-207.
    • (1978) Advan. Biophys. , vol.10 , pp. 137-207
    • Edsall, J.T.1    McKenzie, H.A.2
  • 9
    • 0024745871 scopus 로고
    • The price of lost freedom: Entropy of bimolecular complex formation
    • Finkelstein A. V., Janin J. The price of lost freedom: entropy of bimolecular complex formation. Protein Eng. 3:1989;1-3.
    • (1989) Protein Eng. , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 10
    • 0026326620 scopus 로고
    • Proposed structure for the DNA-binding domain of the Myb oncoprotein based on model building and mutational analysis
    • Frampton J., Gibson T. J., Ness S. A., Doderlein G., Graf T. Proposed structure for the DNA-binding domain of the Myb oncoprotein based on model building and mutational analysis. Protein Eng. 4:1991;891-901.
    • (1991) Protein Eng. , vol.4 , pp. 891-901
    • Frampton, J.1    Gibson, T.J.2    Ness, S.A.3    Doderlein, G.4    Graf, T.5
  • 11
    • 0031576995 scopus 로고    scopus 로고
    • Thermodynamics of the interactions of lac repressor with variants of the symmetric lac operator: Effects of converting a consensus site to a non-specific site
    • Frank D. E., Saecker R. M., Bond J. P., Capp M. W., Tsodikov O. V., Melcher S. E., Levandoski M. M., Record M. T. Jr. Thermodynamics of the interactions of lac repressor with variants of the symmetric lac operator: effects of converting a consensus site to a non-specific site. J. Mol. Biol. 267:1997;1186-1206.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1186-1206
    • Frank, D.E.1    Saecker, R.M.2    Bond, J.P.3    Capp, M.W.4    Tsodikov, O.V.5    Melcher, S.E.6    Levandoski, M.M.7    Record M.T., Jr.8
  • 12
    • 0031552366 scopus 로고    scopus 로고
    • Thermodynamics of the interaction of barnase and barster: Changes in free energy versus changes in enthalpy on mutation
    • Frisch C., Schreiber G., Johnson C. M., Fersht A. R. Thermodynamics of the interaction of barnase and barster: changes in free energy versus changes in enthalpy on mutation. J. Mol. Biol. 267:1997;696-706.
    • (1997) J. Mol. Biol. , vol.267 , pp. 696-706
    • Frisch, C.1    Schreiber, G.2    Johnson, C.M.3    Fersht, A.R.4
  • 13
    • 0026418309 scopus 로고
    • Specific DNA binding by c-Myb: Evidence for a double helix-turn-helix related motif
    • Gabrielsen O. S., Sentenac A., Fromageot P. Specific DNA binding by c-Myb: evidence for a double helix-turn-helix related motif. Science. 253:1991;1140-1143.
    • (1991) Science , vol.253 , pp. 1140-1143
    • Gabrielsen, O.S.1    Sentenac, A.2    Fromageot, P.3
  • 14
    • 0022110525 scopus 로고
    • Nucleotide sequence of cDNA clones of the murine myb protooncogene
    • Gonda T. J., Gough N. M., Dunn A. R., de Blaquiere J. Nucleotide sequence of cDNA clones of the murine myb protooncogene. EMBO J. 4:1985;2003-2008.
    • (1985) EMBO J. , vol.4 , pp. 2003-2008
    • Gonda, T.J.1    Gough, N.M.2    Dunn, A.R.3    De Blaquiere, J.4
  • 17
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha J.-H., Spolar R. S., Record M. T. Jr. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209:1989;801-816.
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.-H.1    Spolar, R.S.2    Record M.T., Jr.3
  • 18
    • 0029808774 scopus 로고    scopus 로고
    • The importance of the linker connecting the repeats of the c-Myb oncoprotein may be due to a positioning function
    • Hegvold A. B., Gabrielsen O. S. The importance of the linker connecting the repeats of the c-Myb oncoprotein may be due to a positioning function. Nucl. Acids Res. 24:1996;3990-3995.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 3990-3995
    • Hegvold, A.B.1    Gabrielsen, O.S.2
  • 19
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz A., Serrano L., Avron B., Bycroft M., Fersht A. R. Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216:1990;1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 20
    • 0025037867 scopus 로고
    • Characterization of the sequence-specific interaction of mouse c- myb protein with DNA
    • Howe K. M., Reakes C. F. L., Watson R. J. Characterization of the sequence-specific interaction of mouse c- myb protein with DNA. EMBO J. 9:1990;161-169.
    • (1990) EMBO J. , vol.9 , pp. 161-169
    • Howe, K.M.1    Reakes, C.F.L.2    Watson, R.J.3
  • 21
    • 0028946647 scopus 로고
    • Thermodynamic evaluation of binding interactions in the methionine receptor system of Escherichia coli using isothermal titration calorimetry
    • Hyre D. E., Spicer L. D. Thermodynamic evaluation of binding interactions in the methionine receptor system of Escherichia coli using isothermal titration calorimetry. Biochemistry. 34:1995;3212-3221.
    • (1995) Biochemistry , vol.34 , pp. 3212-3221
    • Hyre, D.E.1    Spicer, L.D.2
  • 22
    • 0027317958 scopus 로고
    • Thermodynamics of ligand binding to trp repressor
    • Jin L., Yang J., Carey J. Thermodynamics of ligand binding to trp repressor. Biochemistry. 32:1993;7302-7309.
    • (1993) Biochemistry , vol.32 , pp. 7302-7309
    • Jin, L.1    Yang, J.2    Carey, J.3
  • 24
    • 0026803109 scopus 로고
    • Stabilization of Escherichia coli Ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart
    • Kimura S., Nakamura H., Hashimoto T., Oobatake M., Kanaya S. Stabilization of Escherichia coli Ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. J. Biol. Chem. 267:1992;21535-21542.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21535-21542
    • Kimura, S.1    Nakamura, H.2    Hashimoto, T.3    Oobatake, M.4    Kanaya, S.5
  • 25
    • 0030025170 scopus 로고    scopus 로고
    • Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage
    • Klemm J. D., Pabo C. O. Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage. Genes Dev. 10:1996;27-36.
    • (1996) Genes Dev. , vol.10 , pp. 27-36
    • Klemm, J.D.1    Pabo, C.O.2
  • 26
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • Klemm J. D., Rould M. A., Aurora R., Herr W., Pabo C. O. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell. 77:1994;21-32.
    • (1994) Cell , vol.77 , pp. 21-32
    • Klemm, J.D.1    Rould, M.A.2    Aurora, R.3    Herr, W.4    Pabo, C.O.5
  • 27
    • 0023411757 scopus 로고
    • The highly conserved amino-terminal region of the protein encoded by the v- myb oncogene functions as a DNA-binding domain
    • Klempnauer K.-H., Sippel A. E. The highly conserved amino-terminal region of the protein encoded by the v- myb oncogene functions as a DNA-binding domain. EMBO J. 6:1987;2719-2725.
    • (1987) EMBO J. , vol.6 , pp. 2719-2725
    • Klempnauer, K.-H.1    Sippel, A.E.2
  • 28
    • 0029963828 scopus 로고    scopus 로고
    • The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA
    • König P., Giraldo R., Chapman L., Rhodes D. The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. Cell. 85:1996;125-136.
    • (1996) Cell , vol.85 , pp. 125-136
    • König, P.1    Giraldo, R.2    Chapman, L.3    Rhodes, D.4
  • 29
  • 30
    • 0029804729 scopus 로고    scopus 로고
    • Antibody characterization by isothermal titration calorimetry
    • Livingstone J. R. Antibody characterization by isothermal titration calorimetry. Nature. 384:1996;491-492.
    • (1996) Nature , vol.384 , pp. 491-492
    • Livingstone, J.R.1
  • 31
    • 0025906146 scopus 로고
    • Contribution of the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area
    • Livingstone J. R., Spolar R. S., Record M. T. Jr. Contribution of the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry. 30:1991;4237-4244.
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record M.T., Jr.3
  • 32
    • 0030995171 scopus 로고    scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies. III
    • Liu Y., Sturtevant J. M. Significant discrepancies between van't Hoff and calorimetric enthalpies. III. Biophys. Chem. 64:1997;121-126.
    • (1997) Biophys. Chem. , vol.64 , pp. 121-126
    • Liu, Y.1    Sturtevant, J.M.2
  • 33
    • 0027241925 scopus 로고
    • Thermodynamics of the glucocorticoid receptor-DNA interaction: Binding of wild-type GR DBD to different response elements
    • Lundbäck T., Cairns C., Gustafsson J.-A., Carlstedt-Duke J., Härd T. Thermodynamics of the glucocorticoid receptor-DNA interaction: Binding of wild-type GR DBD to different response elements. Biochemistry. 32:1993;5074-5082.
    • (1993) Biochemistry , vol.32 , pp. 5074-5082
    • Lundbäck, T.1    Cairns, C.2    Gustafsson, J.-A.3    Carlstedt-Duke, J.4    Härd, T.5
  • 34
    • 0029899865 scopus 로고    scopus 로고
    • Sequence-specific DNA-binding dominated by dehydration
    • Lundbäck T., Härd T. Sequence-specific DNA-binding dominated by dehydration. Proc. Natl Acad. Sci., USA. 93:1996;4754-4759.
    • (1996) Proc. Natl Acad. Sci., USA , vol.93 , pp. 4754-4759
    • Lundbäck, T.1    Härd, T.2
  • 36
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration
    • Makhatadze G. I., Privalov P. L. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J. Mol. Biol. 232:1993;639-659.
    • (1993) J. Mol. Biol. , vol.232 , pp. 639-659
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 37
    • 0001373814 scopus 로고
    • Some observations on the hypochromism of DNA
    • Mahler H. R., Kline B., Mehrota B. D. Some observations on the hypochromism of DNA. J. Mol. Biol. 9:1964;801-811.
    • (1964) J. Mol. Biol. , vol.9 , pp. 801-811
    • Mahler, H.R.1    Kline, B.2    Mehrota, B.D.3
  • 38
    • 11644276439 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative properties
    • Manning G. S. Limiting laws and counterion condensation in polyelectrolyte solutions I. Colligative properties. J. Chem. Phys. 51:1969;924-933.
    • (1969) J. Chem. Phys. , vol.51 , pp. 924-933
    • Manning, G.S.1
  • 39
    • 0015274187 scopus 로고
    • On the application of polyelectrolyte "limiting laws" to the helix-coil transition of DNA. I. Excess univalent cations
    • Manning G. S. On the application of polyelectrolyte "Limiting laws" to the helix-coil transition of DNA. I. Excess univalent cations. Biopolymers. 11:1972;937-949.
    • (1972) Biopolymers , vol.11 , pp. 937-949
    • Manning, G.S.1
  • 40
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews B. W., Nicholson H., Becktel W. J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl Acad. Sci., USA. 84:1987;6663-6667.
    • (1987) Proc. Natl Acad. Sci., USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 41
    • 0029044394 scopus 로고
    • Calorimetric analysis of λ cI repressor binding to DNA operator sites
    • Merabet E., Ackers G. K. Calorimetric analysis of λ cI repressor binding to DNA operator sites. Biochemistry. 34:1995;8554-8563.
    • (1995) Biochemistry , vol.34 , pp. 8554-8563
    • Merabet, E.1    Ackers, G.K.2
  • 42
    • 0022409539 scopus 로고
    • Thermodynamic origins of specificity in the lac repressor-operator interaction. Adaptability in the recognition of mutant operator sites
    • Mossing M. C., Record M. T. Jr. Thermodynamic origins of specificity in the lac repressor-operator interaction. Adaptability in the recognition of mutant operator sites. J. Mol. Biol. 86:1985;295-305.
    • (1985) J. Mol. Biol. , vol.86 , pp. 295-305
    • Mossing, M.C.1    Record M.T., Jr.2
  • 43
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy K. P., Freire E. Thermodynamics of structural stability and cooperative folding behavior in proteins. Advan. Protein Chem. 43:1992;313-361.
    • (1992) Advan. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 44
    • 0027433604 scopus 로고
    • DNA and redox state induced conformational changes in the DNA-binding domain of the Myb oncoprotein
    • Myrset A. H., Bostad A., Jamin N., Lirsac P.-N., Toma F., Gabrielsen O. S. DNA and redox state induced conformational changes in the DNA-binding domain of the Myb oncoprotein. EMBO J. 12:1993;4625-4633.
    • (1993) EMBO J. , vol.12 , pp. 4625-4633
    • Myrset, A.H.1    Bostad, A.2    Jamin, N.3    Lirsac, P.-N.4    Toma, F.5    Gabrielsen, O.S.6
  • 45
    • 0029064484 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • Naghibi H., Tamura A., Sturtevant J. M. Significant discrepancies between van't Hoff and calorimetric enthalpies. Proc. Natl Acad. Sci. USA. 92:1995;5597-5599.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5597-5599
    • Naghibi, H.1    Tamura, A.2    Sturtevant, J.M.3
  • 46
    • 0030787086 scopus 로고    scopus 로고
    • Investigation of the pyrimidine preference by the c-Myb DNA-binding domain at the initial base of the consensus sequence
    • Oda M., Furukawa K., Ogata K., Sarai A., Ishii S., Nishimura Y., Nakamura H. Investigation of the pyrimidine preference by the c-Myb DNA-binding domain at the initial base of the consensus sequence. J. Biol. Chem. 272:1997a;17966-17971.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17966-17971
    • Oda, M.1    Furukawa, K.2    Ogata, K.3    Sarai, A.4    Ishii, S.5    Nishimura, Y.6    Nakamura, H.7
  • 47
    • 0031430827 scopus 로고    scopus 로고
    • Identification of indispensable residues for specific DNA-binding in the imperfect tandem repeats of c-Myb R2R3
    • Oda M., Furukawa K., Ogata K., Sarai A., Ishii S., Nishimura Y., Nakamura H. Identification of indispensable residues for specific DNA-binding in the imperfect tandem repeats of c-Myb R2R3. Protein Eng. 10:1997b;in the press.
    • (1997) Protein Eng. , vol.10
    • Oda, M.1    Furukawa, K.2    Ogata, K.3    Sarai, A.4    Ishii, S.5    Nishimura, Y.6    Nakamura, H.7
  • 48
    • 0026776412 scopus 로고
    • Solution structure of a DNA-binding unit of Myb: A helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core
    • Ogata K., Hojo H., Aimoto S., Nakai T., Nakamura H., Sarai A., Ishii S., Nishimura Y. Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core. Proc. Natl Acad. Sci. USA. 89:1992;6428-6432.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6428-6432
    • Ogata, K.1    Hojo, H.2    Aimoto, S.3    Nakai, T.4    Nakamura, H.5    Sarai, A.6    Ishii, S.7    Nishimura, Y.8
  • 49
    • 0028138773 scopus 로고
    • Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices
    • Ogata K., Morikawa S., Nakamura H., Sekikawa A., Inoue T., Kanai H., Sarai A., Ishii S., Nishimura Y. Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices. Cell. 79:1994;639-648.
    • (1994) Cell , vol.79 , pp. 639-648
    • Ogata, K.1    Morikawa, S.2    Nakamura, H.3    Sekikawa, A.4    Inoue, T.5    Kanai, H.6    Sarai, A.7    Ishii, S.8    Nishimura, Y.9
  • 52
    • 0027349239 scopus 로고
    • Hydration and heat stability effects on protein unfolding
    • Oobatake M., Ooi T. Hydration and heat stability effects on protein unfolding. Prog. Biophys. Mol. Biol. 59:1993;237-284.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 237-284
    • Oobatake, M.1    Ooi, T.2
  • 53
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo C. O., Sauer R. T. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61:1992;1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 54
  • 55
    • 0026323912 scopus 로고
    • Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA
    • Record M. T. Jr, Ha J.-H., Fisher M. A. Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA. Methods Enzymol. 208:1991;291-343.
    • (1991) Methods Enzymol. , vol.208 , pp. 291-343
    • Record M.T., Jr.1    Ha, J.-H.2    Fisher, M.A.3
  • 56
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards F. M. Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6:1977;151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 57
    • 0025087145 scopus 로고
    • Role of tryptophan repeats and franking amino acids in Myb-DNA interactions
    • Saikumar P., Murali R., Reddy E. P. Role of tryptophan repeats and franking amino acids in Myb-DNA interactions. Proc. Natl Acad. Sci. USA. 87:1990;8452-8456.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8452-8456
    • Saikumar, P.1    Murali, R.2    Reddy, E.P.3
  • 58
    • 0000257239 scopus 로고
    • Delineation of three functional domains of the transcriptional activator encoded by the c- myb protooncogene
    • Sakura H., Kanei-Ishii C., Nagase T., Nakagoshi H., Gonda T. J., Ishii S. Delineation of three functional domains of the transcriptional activator encoded by the c- myb protooncogene. Proc. Natl Acad. Sci. USA. 86:1989;5758-5762.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5758-5762
    • Sakura, H.1    Kanei-Ishii, C.2    Nagase, T.3    Nakagoshi, H.4    Gonda, T.J.5    Ishii, S.6
  • 59
    • 0000127073 scopus 로고
    • Sequence-specific recognition of double helical nucleic acids by proteins
    • Seeman N. C., Rosenberg J. M., Rich A. Sequence-specific recognition of double helical nucleic acids by proteins. Proc. Natl Acad. Sci. USA. 73:1976;804-808.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 804-808
    • Seeman, N.C.1    Rosenberg, J.M.2    Rich, A.3
  • 60
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake A., Rupley J. A. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79:1973;351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 61
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar R. S., Livingstone J. R., Record M. T. Jr. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry. 31:1992;3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record M.T., Jr.3
  • 62
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R. S., Record M. T. Jr. 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., Jr.2
  • 63
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant J. M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl Acad. Sci. USA. 74:1977;2236-2240.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 65
    • 0027361377 scopus 로고
    • Recognition of specific DNA sequences by the c- myb protooncogene product: Role of three repeat units in the DNA-binding domain
    • Tanikawa J., Yasukawa T., Enari M., Ogata K., Nishimura Y., Ishii S., Sarai A. Recognition of specific DNA sequences by the c- myb protooncogene product: role of three repeat units in the DNA-binding domain. Proc. Natl Acad. Sci. USA. 90:1993;9320-9324.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9320-9324
    • Tanikawa, J.1    Yasukawa, T.2    Enari, M.3    Ogata, K.4    Nishimura, Y.5    Ishii, S.6    Sarai, A.7
  • 66
    • 0029085689 scopus 로고
    • The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody
    • Torigoe H., Nakayama T., Imazato M., Shimada I., Arata Y., Sarai A. The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody. J. Biol. Chem. 270:1995;22218-22222.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22218-22222
    • Torigoe, H.1    Nakayama, T.2    Imazato, M.3    Shimada, I.4    Arata, Y.5    Sarai, A.6
  • 67
    • 0002098922 scopus 로고
    • DNA conformation and configuration in protein-DNA complexes
    • Travers A. A. DNA conformation and configuration in protein-DNA complexes. Curr. Opin. Struct. Biol. 2:1992;71-77.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 71-77
    • Travers, A.A.1
  • 68
    • 0026703932 scopus 로고
    • Extension of the DNA binding consensus of the chicken c-Myb and v-Myb proteins
    • Weston K. Extension of the DNA binding consensus of the chicken c-Myb and v-Myb proteins. Nucl. Acids Res. 20:1992;3043-3049.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 3043-3049
    • Weston, K.1
  • 69
    • 0000369599 scopus 로고    scopus 로고
    • Reversible interactions of nucleic acids with small molecules
    • G.M. Blackburn, & M.J. Gait. Oxford: Oxford University Press
    • Wilson W. D. Reversible interactions of nucleic acids with small molecules. Blackburn G. M., Gait M. J. Nucleic acids in Chemistry and Biology. 1996;331-374 Oxford University Press, Oxford.
    • (1996) Nucleic Acids in Chemistry and Biology , pp. 331-374
    • Wilson, W.D.1
  • 70
    • 0024356301 scopus 로고
    • Rapid measurements of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J. F., Lin L. Rapid measurements of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.4
  • 71
    • 0028919759 scopus 로고
    • Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations
    • Xu W., Rould M. A., Jun S., Desplan C., Pabo C. O. Crystal structure of a paired domain-DNA complex at 2.5 Å resolution reveals structural basis for Pax developmental mutations. Cell. 80:1995;639-650.
    • (1995) Cell , vol.80 , pp. 639-650
    • Xu, W.1    Rould, M.A.2    Jun, S.3    Desplan, C.4    Pabo, C.O.5
  • 72
    • 0026099553 scopus 로고
    • Role of conserved proline residues in stabilizing tryptophan synthase subunit: Analysis by mutants with alanine or glycine
    • Yutani K., Hayashi S., Sugisaki Y., Ogasahara K. Role of conserved proline residues in stabilizing tryptophan synthase subunit: analysis by mutants with alanine or glycine. Proteins: Struct. Funct. Genet. 9:1991;90-98.
    • (1991) Proteins: Struct. Funct. Genet. , vol.9 , pp. 90-98
    • Yutani, K.1    Hayashi, S.2    Sugisaki, Y.3    Ogasahara, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.