메뉴 건너뛰기




Volumn 43, Issue 3, 2005, Pages 331-353

The nucleotide-binding site of the Escherichia coli DnaC protein: Molecular topography of DnaC protein-nucleotide cofactor complexes

Author keywords

DNA replication; DnaB helicase; DnaC protein; Motor proteins; Nucleotide binding

Indexed keywords

3' O (N METHYLANTHRANILOYL) ATP; 3' O (N METHYLANTHRANILOYL)ADENOSINE 5' DIPHOSPHATE; 3'-O-(N-METHYLANTHRANILOYL) ATP; 3'-O-(N-METHYLANTHRANILOYL)ADENOSINE 5'-DIPHOSPHATE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANTHRANILIC ACID DERIVATIVE; DNAC PROTEIN, E COLI; DRUG DERIVATIVE; ESCHERICHIA COLI PROTEIN; MAGNESIUM CHLORIDE; TRYPTOPHAN; TYROSINE;

EID: 27144500753     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:43:3:331     Document Type: Article
Times cited : (5)

References (56)
  • 2
    • 0026777126 scopus 로고
    • Prokaryotic DNA replication
    • Marians, K. J. (1992) Prokaryotic DNA replication. Ann. Rev. Biochem. 61, 673-719.
    • (1992) Ann. Rev. Biochem. , vol.61 , pp. 673-719
    • Marians, K.J.1
  • 3
    • 0028838404 scopus 로고
    • The speed of the Escherichia coli fork in vivo depends on the DnaB-DnaC ratio
    • Skarstad, K. and Wold, S. (1995) The speed of the Escherichia coli fork in vivo depends on the DnaB-DnaC ratio. Mol. Microbiol. 17, 825-831.
    • (1995) Mol. Microbiol. , vol.17 , pp. 825-831
    • Skarstad, K.1    Wold, S.2
  • 4
    • 0001266666 scopus 로고
    • Association of DNA-dependent and -independent ribonucleoside triphosphatase activities with dnaB gene product of Escherichia coli
    • Wickner, S., Wright, M., and Hurwitz, J. (1974) Association of DNA-dependent and -independent ribonucleoside triphosphatase activities with dnaB gene product of Escherichia coli. Proc. Natl. Acad. Sci. USA 71, 783-787.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 783-787
    • Wickner, S.1    Wright, M.2    Hurwitz, J.3
  • 5
    • 0000579776 scopus 로고
    • Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro
    • Wickner, S. and Hurwitz, J. (1975) Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro. Proc. Natl. Acad. Sci. US A. 72, 921-925.
    • (1975) Proc. Natl. Acad. Sci. US A , vol.72 , pp. 921-925
    • Wickner, S.1    Hurwitz, J.2
  • 6
    • 0016426540 scopus 로고
    • Genetic and phenotypic characterization of dnaC mutations
    • Wechsler, J. (1975) Genetic and phenotypic characterization of dnaC mutations. J. Bacteriol. 121, 594-599.
    • (1975) J. Bacteriol. , vol.121 , pp. 594-599
    • Wechsler, J.1
  • 7
    • 0015178421 scopus 로고
    • Escherichia coli mutants temperature-sensitive for DNA synthesis
    • Wechsler, J. and Gross, J. D. (1971) Escherichia coli mutants temperature-sensitive for DNA synthesis. Mol. Gen. Genet. 113, 273-284.
    • (1971) Mol. Gen. Genet. , vol.113 , pp. 273-284
    • Wechsler, J.1    Gross, J.D.2
  • 8
    • 0032605883 scopus 로고    scopus 로고
    • PriA: At the crossroads of DNA replication and recombination
    • Marians, K. J. (1999) PriA: at the crossroads of DNA replication and recombination. Prog. Nucl. Acid. Res. Mol. Biol. 63, 39-67.
    • (1999) Prog. Nucl. Acid. Res. Mol. Biol. , vol.63 , pp. 39-67
    • Marians, K.J.1
  • 9
    • 0024562458 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties
    • Wahle, E., Lasken, R. S., and Kornberg, A. (1989) The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties. J. Biol. Chem. 264, 2463-2468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2463-2468
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 10
    • 0024520416 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions
    • Wahle, E., Lasken, R. S., and Kornberg, A. (1989) The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions. J. Biol. Chem. 264, 2469-2475.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2469-2475
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 11
    • 0025876111 scopus 로고
    • The priB gene encoding the primosomal replicative n protein of Escherichia coli
    • Allen, G. C. and Kornberg, A. (1991) The priB gene encoding the primosomal replicative n protein of Escherichia coli. J. Biol. Chem. 266, 22096-22101.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22096-22101
    • Allen, G.C.1    Kornberg, A.2
  • 12
    • 0020356352 scopus 로고
    • The Escherichia coli dnaC gene product. I. Overproduction of the dnaC proteins of Escherichia coli and Salmonella Typhimurium by cloning into a high copy number plasmid
    • Kobori, J. A. and Kornberg, A. (1982) The Escherichia coli dnaC gene product. I. Overproduction of the dnaC proteins of Escherichia coli and Salmonella Typhimurium by cloning into a high copy number plasmid. J. Biol. Chem. 257, 13757-13762.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13757-13762
    • Kobori, J.A.1    Kornberg, A.2
  • 13
    • 0020355756 scopus 로고
    • The Escherichia coli dnaC gene product. II. Purification, physical properties, and role in replication
    • Kobori, J. A. and Kornberg, A. (1982) The Escherichia coli dnaC gene product. II. Purification, physical properties, and role in replication. J. Biol. Chem. 257, 13763-13769.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13763-13769
    • Kobori, J.A.1    Kornberg, A.2
  • 14
    • 0028998688 scopus 로고
    • DnaA-dependent assembly of the ABC primosome at the A site, a single-stranded DNA hairpin containing a dnaA box
    • Masai, H. and Arai, K. (1995) DnaA-dependent assembly of the ABC primosome at the A site, a single-stranded DNA hairpin containing a dnaA box. Eur. J. Biochem. 230, 384-395.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 384-395
    • Masai, H.1    Arai, K.2
  • 15
    • 0035977018 scopus 로고    scopus 로고
    • DnaA protein directs the binding of the DnaB protein in initiation of DNA replication
    • Marszalek, J. and Kaguni, J. M. (2001) DnaA protein directs the binding of the DnaB protein in initiation of DNA replication. J. Biol. Chem. 276, 44919-44925.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44919-44925
    • Marszalek, J.1    Kaguni, J.M.2
  • 16
    • 0029072199 scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer
    • Bujalowski, W. and Jezewska, M. J. (1995) Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer. Biochemistry 34, 8513-8519.
    • (1995) Biochemistry , vol.34 , pp. 8513-8519
    • Bujalowski, W.1    Jezewska, M.J.2
  • 17
    • 0030030309 scopus 로고    scopus 로고
    • A general method of analysis of ligand binding to competing macromolecules using the spectroscopic signal originating from a reference macromolecule. Application to Escherichia coli replicative helicase DnaB protein-nucleic acid interactions
    • Jezewska, M. J. and Bujalowski, W. (1996) A general method of analysis of ligand binding to competing macromolecules using the spectroscopic signal originating from a reference macromolecule. Application to Escherichia coli replicative helicase DnaB protein-nucleic acid interactions. Biochemistry 35, 2117-2128.
    • (1996) Biochemistry , vol.35 , pp. 2117-2128
    • Jezewska, M.J.1    Bujalowski, W.2
  • 18
    • 0030052444 scopus 로고    scopus 로고
    • Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer
    • Jezewska, M. J., Kim, U.-S., and Bujalowski, W. (1996) Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer. Biochemistry 35, 2129-2145.
    • (1996) Biochemistry , vol.35 , pp. 2129-2145
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 19
    • 0032562822 scopus 로고    scopus 로고
    • Does ssDNA pass through the inner channel of the protein hexamer in the complex with the E. coli DnaB helicase? Fluorescence energy transfer studies
    • Jezewska, M. J., Rajendran S., Bujalowska, D., and Bujalowski, W. (1998) Does ssDNA pass through the inner channel of the protein hexamer in the complex with the E. coli DnaB helicase? Fluorescence energy transfer studies, J. Biol. Chem. 273, 10515-10529.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 20
    • 0032502678 scopus 로고    scopus 로고
    • Functional and structural heterogeneity of the DNA binding of the E. coli primary replicative helicase DnaB protein
    • Jezewska, M. J., Rajendran S., and Bujalowski, W. (1998) Functional and structural heterogeneity of the DNA binding of the E. coli primary replicative helicase DnaB protein. J. Biol. Chem. 273, 9058-9069.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 21
    • 0030747747 scopus 로고    scopus 로고
    • Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with replication fork
    • Jezewska, M. J., Rajendran, S., and Bujalowski, W. (1997) Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with replication fork. Biochemistry 36, 10320-10326.
    • (1997) Biochemistry , vol.36 , pp. 10320-10326
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 22
    • 0034711089 scopus 로고    scopus 로고
    • Interactions of nucleotide cofactors with the Escherichia coli replication ractor DnaC protein
    • Galletto, R., Rajendran, S., and Bujalowski, W. (2000) Interactions of nucleotide cofactors with the Escherichia coli replication ractor DnaC protein. Biochemistry 39, 12959-12969.
    • (2000) Biochemistry , vol.39 , pp. 12959-12969
    • Galletto, R.1    Rajendran, S.2    Bujalowski, W.3
  • 23
    • 0037118714 scopus 로고    scopus 로고
    • The E. coli replication factor DnaC protein exists in two conformations with different nucleotide binding capabilities. I. Determination of the binding mechanism using ATP and ADP fluorescent analogs
    • Galletto, R. and Bujalowski, W. (2002) The E. coli replication factor DnaC protein exists in two conformations with different nucleotide binding capabilities. I. Determination of the binding mechanism using ATP and ADP fluorescent analogs. Biochemistry 41, 8907-8920.
    • (2002) Biochemistry , vol.41 , pp. 8907-8920
    • Galletto, R.1    Bujalowski, W.2
  • 24
    • 0037118717 scopus 로고    scopus 로고
    • Kinetics of E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient dynamic quenching stopped-flow studies of the reaction intermediates
    • Galletto, R. and Bujalowski, W. (2002) Kinetics of E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient dynamic quenching stopped-flow studies of the reaction intermediates. Biochemistry 41, 8921-8934.
    • (2002) Biochemistry , vol.41 , pp. 8921-8934
    • Galletto, R.1    Bujalowski, W.2
  • 25
    • 0037616144 scopus 로고    scopus 로고
    • Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on the protein-protein interactions and the topology of the complex
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2003) Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on the protein-protein interactions and the topology of the complex. J. Mol. Biol. 329, 441-465.
    • (2003) J. Mol. Biol. , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 26
    • 0015894660 scopus 로고
    • Preparation and properties of 2′ (or 3′)-O-(2,4,6- trinitrophenyl)adenosine 5′-triphosphate, an analog of adenosine triphosphate
    • Hiratsuka, T. and Uchida, K. (1973) Preparation and properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl)adenosine 5′-triphosphate, an analog of adenosine triphosphate. Biochim. Biophys. Acta 320, 635-647.
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 635-647
    • Hiratsuka, T.1    Uchida, K.2
  • 27
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes, Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 28
    • 0027214787 scopus 로고
    • Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs
    • Bujalowski, W. and Klonowska, M. M. (1993) Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs. Biochemistry 32, 5888-5900.
    • (1993) Biochemistry , vol.32 , pp. 5888-5900
    • Bujalowski, W.1    Klonowska, M.M.2
  • 29
    • 0028207331 scopus 로고
    • Structural characteristics of the nucleotide binding site of the E. coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs
    • Bujalowski, W. and Klonowska, M. M. (1994) Structural characteristics of the nucleotide binding site of the E. coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs. Biochemistry 33, 4682-4694.
    • (1994) Biochemistry , vol.33 , pp. 4682-4694
    • Bujalowski, W.1    Klonowska, M.M.2
  • 30
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein
    • Bujalowski, W., Klonowska, M. M., and Jezewska M. J. (1994) Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 269, 31359-31371.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31359-31371
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 31
    • 0029813340 scopus 로고    scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors
    • Jezewska, M. J., Kim, U.-S., and Bujalowski, W. (1997) Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors. Biophys. J. 71, 2075-2086.
    • (1997) Biophys. J. , vol.71 , pp. 2075-2086
    • Jezewska, M.J.1    Kim, U.-S.2    Bujalowski, W.3
  • 32
    • 33847682952 scopus 로고
    • Correction of fluorescence spectra and measurement of fluorescence quantum efficiency
    • Parker, C. A. and Reese, W. T. (1960) Correction of fluorescence spectra and measurement of fluorescence quantum efficiency. Analyst 85, 587-592.
    • (1960) Analyst , vol.85 , pp. 587-592
    • Parker, C.A.1    Reese, W.T.2
  • 33
    • 30244573126 scopus 로고
    • Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models
    • Scott, T. G., Spencer, R. D., Leonard, N. J., and Weber, G. (1970) Emission properties of NADH. Studies of fluorescence lifetimes and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models. J. Am. Chem. Soc. 92, 687-695.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 687-695
    • Scott, T.G.1    Spencer, R.D.2    Leonard, N.J.3    Weber, G.4
  • 34
    • 36849119614 scopus 로고
    • Polarization of the luminescence of phenanthrene
    • Azumi, T. and McGlynn, S. P. (1962) Polarization of the luminescence of phenanthrene, J. Chem. Phys. 37, 2413-2420.
    • (1962) J. Chem. Phys. , vol.37 , pp. 2413-2420
    • Azumi, T.1    McGlynn, S.P.2
  • 36
    • 0001917250 scopus 로고
    • Fluorescence quenching: Theory and applications
    • (Lakowicz, J. R., ed.). Plenum Press, New York
    • Eftink M. R. (1991) Fluorescence quenching: theory and applications, in Topics in Fluorescence Spectroscopy (Lakowicz, J. R., ed.). Plenum Press, New York, pp. 53-126.
    • (1991) Topics in Fluorescence Spectroscopy , pp. 53-126
    • Eftink, M.R.1
  • 38
    • 0014592780 scopus 로고
    • Intramolecular energy transfer in adrenocorticotropin
    • Eisinger, J. (1969) Intramolecular energy transfer in adrenocorticotropin. Biochemistry 8, 3902-3908.
    • (1969) Biochemistry , vol.8 , pp. 3902-3908
    • Eisinger, J.1
  • 39
    • 84985482714 scopus 로고
    • Excitation energy transfer between tyrosine and tryptophan in proteins evaluated by simultaneous measurement of fluorescence and absorbance
    • Saito, Y., Tachibana, H., Hayashi, H., and Wada, A. (1981) Excitation energy transfer between tyrosine and tryptophan in proteins evaluated by simultaneous measurement of fluorescence and absorbance. Photochem. Photobiol. 33, 289-295.
    • (1981) Photochem. Photobiol. , vol.33 , pp. 289-295
    • Saito, Y.1    Tachibana, H.2    Hayashi, H.3    Wada, A.4
  • 40
    • 0025332536 scopus 로고
    • Interaction of myosin subfragment 1 with fluorescent ribose-modified nucleotides. A comparison of vanadate trapping and SH1-SH2 cross-linking
    • Cremo, C. R., Neuron, J. M., and Yount, R. G. (1990) Interaction of myosin subfragment 1 with fluorescent ribose-modified nucleotides. A comparison of vanadate trapping and SH1-SH2 cross-linking. Biochemistry 29, 3309-3319.
    • (1990) Biochemistry , vol.29 , pp. 3309-3319
    • Cremo, C.R.1    Neuron, J.M.2    Yount, R.G.3
  • 41
    • 0017917406 scopus 로고
    • The use of singlet-singlet energy transfer to study macromolecular assemblies
    • Fairclough, R. H. and Cantor, C. R. (1978) The use of singlet-singlet energy transfer to study macromolecular assemblies. Methods Enzymol. 48, 347-379.
    • (1978) Methods Enzymol. , vol.48 , pp. 347-379
    • Fairclough, R.H.1    Cantor, C.R.2
  • 42
    • 0038290256 scopus 로고    scopus 로고
    • Rat polymerase b binds double-stranded DNA using exclusively the 8-kDa domain. Stoichiometries, intrinsic affinities, and cooperativities
    • Jezewska, M. J., Galletto, R., and Bujalowski, W. (2003) Rat polymerase b binds double-stranded DNA using exclusively the 8-kDa domain. Stoichiometries, intrinsic affinities, and cooperativities. Biochemistry 42, 5955-5970.
    • (2003) Biochemistry , vol.42 , pp. 5955-5970
    • Jezewska, M.J.1    Galletto, R.2    Bujalowski, W.3
  • 43
    • 0032562822 scopus 로고    scopus 로고
    • Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies
    • Jezewska, M. J., Rajendran, S., Bujalowska, D., and Bujalowski, W. (1998) Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies. J. Biol. Chem. 273, 10515-10529.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 44
    • 0035797894 scopus 로고    scopus 로고
    • Multiple-step mechanisms of the ssDNA recognition process by human polymerase b in its different binding modes
    • Rajendran, S., Jezewska, M. J., and Bujalowski, W. (2001) Multiple-step mechanisms of the ssDNA recognition process by human polymerase b in its different binding modes. Biochemistry 40, 11794-11810.
    • (2001) Biochemistry , vol.40 , pp. 11794-11810
    • Rajendran, S.1    Jezewska, M.J.2    Bujalowski, W.3
  • 45
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by second-derivative spectroscopy
    • Ragone, R., Colonna, G., Balestrieri, C., Servillo, L., and Irace, G. (1984) Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 23, 1871-1875.
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 46
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink, M. R. and Ghiron, C.A. (1981) Fluorescence quenching studies with proteins. Anal. Biochem. 14, 199-227.
    • (1981) Anal. Biochem. , vol.14 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 47
    • 0017348776 scopus 로고
    • A hydrophobic quencher of protein fluorescence: 2,2,2-trichloroethanol
    • Eftink, M. R., Zajicek, J. L., and Ghiron, C. A. (1977) A hydrophobic quencher of protein fluorescence: 2,2,2-trichloroethanol. Biochim. Biophys. Acta 491, 473-481.
    • (1977) Biochim. Biophys. Acta , vol.491 , pp. 473-481
    • Eftink, M.R.1    Zajicek, J.L.2    Ghiron, C.A.3
  • 48
    • 77956741418 scopus 로고
    • Ultraviolet absorption spectra of proteins and amino acids
    • Wetlaufer, D. B. (1962) Ultraviolet absorption spectra of proteins and amino acids. Advan. Protein Chem. 17, 303-390.
    • (1962) Advan. Protein Chem. , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 49
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules
    • Lakowicz, J. and Weber, G. (1973) Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry 12, 4161-4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.1    Weber, G.2
  • 50
    • 0021769550 scopus 로고
    • 2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP
    • 2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP. Biochemistry 23, 5262-5271.
    • (1984) Biochemistry , vol.23 , pp. 5262-5271
    • Pecoraro, V.L.1    Hermes, J.D.2    Cleland, W.W.3
  • 51
    • 0023645239 scopus 로고
    • Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein
    • Nakayama, N., Bond, M. W., Miyajima, A., Kobori, J., and Arai, K. (1987) Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein. J. Biol. Chem. 262, 10475-10480.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10475-10480
    • Nakayama, N.1    Bond, M.W.2    Miyajima, A.3    Kobori, J.4    Arai, K.5
  • 53
    • 0000944228 scopus 로고
    • Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds
    • Weber, G. (1960) Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds. Biochem J. 75, 335-345.
    • (1960) Biochem. J. , vol.75 , pp. 335-345
    • Weber, G.1
  • 54
    • 4644257077 scopus 로고    scopus 로고
    • Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors
    • Galletto, R., Maillard, R., Jezewska, M. J., and Bujalowski, W. (2004) Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors. Biochemistry 43, 10988-11001.
    • (2004) Biochemistry , vol.43 , pp. 10988-11001
    • Galletto, R.1    Maillard, R.2    Jezewska, M.J.3    Bujalowski, W.4
  • 55
    • 0018804403 scopus 로고
    • Estimation of state and amount of phenylalanine residues in proteins by second derivative Spectrophotometry
    • Ichikawa, T. and Terada, H. (1979) Estimation of state and amount of phenylalanine residues in proteins by second derivative Spectrophotometry. Biochim. Biophys. Acta 580, 120-128.
    • (1979) Biochim. Biophys. Acta , vol.580 , pp. 120-128
    • Ichikawa, T.1    Terada, H.2
  • 56
    • 0017402866 scopus 로고
    • Second derivative spectrophotometry as an effective tool for examining phenylalanine residues in proteins
    • Ichikawa, T., and Terada, H. (1977) Second derivative spectrophotometry as an effective tool for examining phenylalanine residues in proteins. Biochim. Biophys. Acta 494, 267-270.
    • (1977) Biochim. Biophys. Acta , vol.494 , pp. 267-270
    • Ichikawa, T.1    Terada, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.