메뉴 건너뛰기




Volumn 159, Issue 1, 2011, Pages 48-57

E. coli SSB tetramer binds the first and second molecules of (dT) 35 with heat capacities of opposite sign

Author keywords

EcoSSB; ITC; Opposite heat capacity effect; Salt dependence; SSB ssDNA thermodynamics; ssDNA binding

Indexed keywords

OLIGODEOXYNUCLEOTIDE; SINGLE STRANDED DNA BINDING PROTEIN; SODIUM CHLORIDE;

EID: 80052328404     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.05.005     Document Type: Article
Times cited : (9)

References (50)
  • 1
    • 0022555837 scopus 로고
    • Single-stranded DNA binding proteins required for DNA replication
    • J.W. Chase, and K.R. Williams Single-stranded DNA binding proteins required for DNA replication Annu. Rev. Biochem. 55 1986 103 136 (Pubitemid 16070765)
    • (1986) Annual Review of Biochemistry , vol.55 , pp. 103-136
    • Chase, J.W.1    Williams, K.R.2
  • 3
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • R.R. Meyer, and P.S. Laine The single-stranded DNA-binding protein of Escherichia coli Microbiol. Rev. 54 1990 342 380 (Pubitemid 120004379)
    • (1990) Microbiological Reviews , vol.54 , Issue.4 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 4
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • T.M. Lohman, and M.E. Ferrari Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities Annu. Rev. Biochem. 63 1994 527 570
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 5
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution
    • S. Raghunathan, C.S. Ricard, T.M. Lohman, and G. Waksman Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution Proc. Natl. Acad. Sci. U. S. A. 94 1997 6652 6657
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 6
    • 0033887437 scopus 로고    scopus 로고
    • Structure of the DNA binding domain of E. coli SSB bound to ssDNA
    • DOI 10.1038/77943
    • S. Raghunathan, A.G. Kozlov, T.M. Lohman, and G. Waksman Structure of the DNA binding domain of E-coli SSB bound to ssDNA Nat. Struct. Biol. 7 2000 648 652 (Pubitemid 30636675)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 648-652
    • Raghunathan, S.1    Kozlov, A.G.2    Lohman, T.M.3    Waksman, G.4
  • 7
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration
    • T.M. Lohman, and L.B. Overman Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration J. Biol. Chem. 260 1985 3594 3603 (Pubitemid 15114361)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.6 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 8
    • 0023040461 scopus 로고
    • Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA
    • W. Bujalowski, and T.M. Lohman Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA Biochemistry 25 1986 7799 7802
    • (1986) Biochemistry , vol.25 , pp. 7799-7802
    • Bujalowski, W.1    Lohman, T.M.2
  • 11
    • 0023916373 scopus 로고
    • Binding mode transitions of Escherichia coli single strand binding protein-single-stranded DNA complexes. Cation, anion, pH, and binding density effects
    • W. Bujalowski, L.B. Overman, and T.M. Lohman Binding mode transitions of Escherichia coli single strand binding protein-single-stranded DNA complexes. Cation, anion, pH, and binding density effects J. Biol. Chem. 263 1988 4629 4640
    • (1988) J. Biol. Chem. , vol.263 , pp. 4629-4640
    • Bujalowski, W.1    Overman, L.B.2    Lohman, T.M.3
  • 12
    • 34248664689 scopus 로고    scopus 로고
    • Dynamic Structural Rearrangements Between DNA Binding Modes of E. coli SSB Protein
    • DOI 10.1016/j.jmb.2007.03.079, PII S0022283607004561
    • R. Roy, A.G. Kozlov, T.M. Lohman, and T. Ha Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein J. Mol. Biol. 369 2007 1244 1257 (Pubitemid 46770769)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.5 , pp. 1244-1257
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 13
    • 0022542165 scopus 로고
    • Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein
    • T.M. Lohman, L.B. Overman, and S. Datta Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein J. Mol. Biol. 187 1986 603 615 (Pubitemid 16041061)
    • (1986) Journal of Molecular Biology , vol.187 , Issue.4 , pp. 603-615
    • Lohman, T.M.1    Overman, L.B.2    Datta, S.3
  • 15
    • 0028175289 scopus 로고
    • Co-operative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB)35 binding mode
    • M.E. Ferrari, W. Bujalowski, and T.M. Lohman Co-operative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB)35 binding mode J. Mol. Biol. 236 1994 106 123
    • (1994) J. Mol. Biol. , vol.236 , pp. 106-123
    • Ferrari, M.E.1    Bujalowski, W.2    Lohman, T.M.3
  • 16
    • 3042625942 scopus 로고    scopus 로고
    • The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA
    • DOI 10.1110/ps.04661904
    • S.N. Savvides, S. Raghunathan, K. Futterer, A.G. Kozlov, T.M. Lohman, and G. Waksman The C-terminal domain of full-length E-coli SSB is disordered even when bound to DNA Protein Sci. 13 2004 1942 1947 (Pubitemid 38822135)
    • (2004) Protein Science , vol.13 , Issue.7 , pp. 1942-1947
    • Savvides, S.N.1    Raghunathan, S.2    Futterer, K.3    Kozlov, A.G.4    Lohman, T.M.5    Waksman, G.6
  • 17
    • 77951690386 scopus 로고    scopus 로고
    • Binding specificity of Escherichia coli single-stranded DNA binding protein for the chi subunit of DNA pol III holoenzyme and PriA helicase
    • A.G. Kozlov, M.J. Jezewska, W. Bujalowski, and T.M. Lohman Binding specificity of Escherichia coli single-stranded DNA binding protein for the chi subunit of DNA pol III holoenzyme and PriA helicase Biochemistry 49 2010 3555 3566
    • (2010) Biochemistry , vol.49 , pp. 3555-3566
    • Kozlov, A.G.1    Jezewska, M.J.2    Bujalowski, W.3    Lohman, T.M.4
  • 18
    • 77952783935 scopus 로고    scopus 로고
    • Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein
    • A.G. Kozlov, M.M. Cox, and T.M. Lohman Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein J. Biol. Chem. 285 2010 17246 17252
    • (2010) J. Biol. Chem. , vol.285 , pp. 17246-17252
    • Kozlov, A.G.1    Cox, M.M.2    Lohman, T.M.3
  • 19
    • 70350488396 scopus 로고    scopus 로고
    • SSB protein diffusion on single-stranded DNA stimulates RecA filament formation
    • R. Roy, A.G. Kozlov, T.M. Lohman, and T. Ha SSB protein diffusion on single-stranded DNA stimulates RecA filament formation Nature 461 2009 1092 1097
    • (2009) Nature , vol.461 , pp. 1092-1097
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 20
    • 0024403429 scopus 로고
    • Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model
    • DOI 10.1016/0022-2836(89)90454-3
    • W. Bujalowski, and T.M. Lohman Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model J. Mol. Biol. 207 1989 249 268 (Pubitemid 19141255)
    • (1989) Journal of Molecular Biology , vol.207 , Issue.1 , pp. 249-268
    • Bujalowski, W.1    Lohman, T.M.2
  • 21
    • 0024356728 scopus 로고
    • Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effects
    • DOI 10.1016/0022-2836(89)90455-5
    • W. Bujalowski, and T.M. Lohman Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effects J. Mol. Biol. 207 1989 269 288 (Pubitemid 19141256)
    • (1989) Journal of Molecular Biology , vol.207 , Issue.1 , pp. 269-288
    • Bujalowski, W.1    Lohman, T.M.2
  • 22
    • 0028358069 scopus 로고
    • Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single-stranded DNA complexes
    • DOI 10.1021/bi00186a016
    • T.M. Lohman, and W. Bujalowski Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single-stranded DNA complexes Biochemistry 33 1994 6167 6176 (Pubitemid 24190768)
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6167-6176
    • Lohman, T.M.1    Bujalowski, W.2
  • 23
    • 0032557719 scopus 로고    scopus 로고
    • Calorimetric studies of E. coli SSB protein-single-stranded DNA interactions. Effects of monovalent salts on binding enthalpy
    • DOI 10.1006/jmbi.1998.1738
    • A.G. Kozlov, and T.M. Lohman Calorimetric studies of E-coli SSB protein single-stranded DNA interactions. Effects of monovalent salts on binding enthalpy J. Mol. Biol. 278 1998 999 1014 (Pubitemid 28239700)
    • (1998) Journal of Molecular Biology , vol.278 , Issue.5 , pp. 999-1014
    • Kozlov, A.G.1    Lohman, T.M.2
  • 24
    • 0033153360 scopus 로고    scopus 로고
    • Adenine base unstacking dominates the observed enthalpy and heat capacity changes for the Escherichia coli SSB tetramer binding to single-stranded oligoadenylates
    • A.G. Kozlov, and T.M. Lohman Adenine base unstacking dominates the observed enthalpy and heat capacity changes for the Escherichia coli SSB tetramer binding to single-stranded oligoadenylates Biochemistry 38 1999 7388 7397
    • (1999) Biochemistry , vol.38 , pp. 7388-7397
    • Kozlov, A.G.1    Lohman, T.M.2
  • 25
    • 0033780671 scopus 로고    scopus 로고
    • Large contributions of coupled protonation equilibria to the observed enthalpy and heat capacity changes for ssDNA binding to Escherichia coli SSB protein
    • A.G. Kozlov, and T.M. Lohman Large contributions of coupled protonation equilibria to the observed enthalpy and heat capacity changes for ssDNA binding to Escherichia coli SSB protein Proteins Suppl. 4 2000 8 22
    • (2000) Proteins , Issue.SUPPL. 4 , pp. 8-22
    • Kozlov, A.G.1    Lohman, T.M.2
  • 26
    • 0037076536 scopus 로고    scopus 로고
    • Stopped-flow studies of the kinetics of single-stranded DNA binding and wrapping around the Escherichia coli SSB tetramer
    • DOI 10.1021/bi020122z
    • A.G. Kozlov, and T.M. Lohman Stopped-flow studies of the kinetics of single-stranded DNA binding and wrapping around the Escherichia coli SSB tetramer Biochemistry 41 2002 6032 6044 (Pubitemid 34498909)
    • (2002) Biochemistry , vol.41 , Issue.19 , pp. 6032-6044
    • Kozlov, A.G.1    Lohman, T.M.2
  • 27
    • 33645971001 scopus 로고    scopus 로고
    • Effects of monovalent anions on a temperature-dependent heat capacity change for Escherichia coli SSB tetramer binding to single-stranded DNA
    • A.G. Kozlov, and T.M. Lohman Effects of monovalent anions on a temperature-dependent heat capacity change for Escherichia coli SSB tetramer binding to single-stranded DNA Biochemistry 45 2006 5190 5205
    • (2006) Biochemistry , vol.45 , pp. 5190-5205
    • Kozlov, A.G.1    Lohman, T.M.2
  • 28
    • 0029933128 scopus 로고    scopus 로고
    • A highly salt-dependent enthalpy change for Escherichia coli SSB protein-nucleic acid binding due to ion-protein interactions
    • T.M. Lohman, L.B. Overman, M.E. Ferrari, and A.G. Kozlov A highly salt-dependent enthalpy change for Escherichia coli SSB protein-nucleic acid binding due to ion-protein interactions Biochemistry 35 1996 5272 5279
    • (1996) Biochemistry , vol.35 , pp. 5272-5279
    • Lohman, T.M.1    Overman, L.B.2    Ferrari, M.E.3    Kozlov, A.G.4
  • 29
    • 0031670461 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride
    • DOI 10.1002/(SICI)1097-0134(19981101)33:2<159::AID-PROT2>3.0.CO;2-E
    • H. Fukada, and K. Takahashi Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride Proteins 33 1998 159 166 (Pubitemid 28457970)
    • (1998) Proteins: Structure, Function and Genetics , vol.33 , Issue.2 , pp. 159-166
    • Fukada, H.1    Takahashi, K.2
  • 31
    • 0022493915 scopus 로고
    • Large-scale overproduction and rapid purification of the Escherichia coli ssb gene product. Expression of the ssb gene under λ P(L) control
    • T.M. Lohman, J.M. Green, and R.S. Beyer Large-scale overproduction and rapid purification of the Escherichia coli ssb gene product. Expression of the ssb gene under lambda PL control Biochemistry 25 1986 21 25 (Pubitemid 16053074)
    • (1986) Biochemistry , vol.25 , Issue.1 , pp. 21-25
    • Lohman, T.M.1    Green, J.M.2    Beyer, R.S.3
  • 32
    • 0026078480 scopus 로고
    • Monomer-tetramer equilibrium of the Escherichia coli ssb-1 mutant single strand binding protein
    • W. Bujalowski, and T.M. Lohman Monomer-tetramer equilibrium of the Escherichia coli ssb-1 mutant single strand binding protein J. Biol. Chem. 266 1991 1616 1626 (Pubitemid 21908346)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.3 , pp. 1616-1626
    • Bujalowski, W.1    Lohman, T.M.2
  • 33
    • 0024284762 scopus 로고
    • Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB)65 binding mode. Cation and anion effects and polynucleotide specificity
    • L.B. Overman, W. Bujalowski, and T.M. Lohman Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB)65 binding mode. Cation and anion effects and polynucleotide specificity Biochemistry 27 1988 456 471
    • (1988) Biochemistry , vol.27 , pp. 456-471
    • Overman, L.B.1    Bujalowski, W.2    Lohman, T.M.3
  • 34
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • DOI 10.1016/0022-2836(81)90335-1
    • S.C. Kowalczykowski, N. Lonberg, J.W. Newport, and P.H. von Hippel Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions J. Mol. Biol. 145 1981 75 104 (Pubitemid 11189055)
    • (1981) Journal of Molecular Biology , vol.145 , Issue.1 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.H.4
  • 35
    • 0000290004 scopus 로고
    • Transitions of DNA homopolymers
    • R.B. Inman Transitions of DNA homopolymers J. Mol. Biol. 9 1964 624 637
    • (1964) J. Mol. Biol. , vol.9 , pp. 624-637
    • Inman, R.B.1
  • 36
    • 0001416060 scopus 로고
    • Single-stranded oligomers and polymers of cytidylic and 2′-deoxycytidylic acids: Comparative optical rotatory studies
    • B.A. Adler, L. Grossman, and G.D. Fasman Single-stranded oligomers and polymers of cytidylic and 2′-deoxycytidylic acids: comparative optical rotatory studies Proc. Natl. Acad. Sci. U. S. A. 57 1967 423 430
    • (1967) Proc. Natl. Acad. Sci. U. S. A. , vol.57 , pp. 423-430
    • Adler, B.A.1    Grossman, L.2    Fasman, G.D.3
  • 37
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 131 137 (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 39
    • 0021093448 scopus 로고
    • Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • M.R. Eftink, A.C. Anusiem, and R.L. Biltonen Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A Biochemistry 22 1983 3884 3896
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 40
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • DOI 10.1016/0022-2836(89)90608-6
    • J.H. Ha, R.S. Spolar, and M.T. Record Jr. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes J. Mol. Biol. 209 1989 801 816 (Pubitemid 20046133)
    • (1989) Journal of Molecular Biology , vol.209 , Issue.4 , pp. 801-816
    • Ha, J.-H.1    Spolar, R.S.2    Record Jr., M.T.3
  • 41
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • K.P. Murphy, and E. Freire Thermodynamics of structural stability and cooperative folding behavior in proteins Adv. Protein Chem. 43 1992 313 361
    • (1992) Adv. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 42
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • R.S. Spolar, and M.T. Record Jr. Coupling of local folding to site-specific binding of proteins to DNA Science 263 1994 777 784 (Pubitemid 24093205)
    • (1994) Science , vol.263 , Issue.5148 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 43
    • 0029860343 scopus 로고    scopus 로고
    • Water mediated protein-DNA interactions: The relationship of thermodynamics to structural detail
    • C.J. Morton, and J.E. Ladbury Water-mediated protein-DNA interactions: the relationship of thermodynamics to structural detail Protein Sci. 5 1996 2115 2118 (Pubitemid 26347747)
    • (1996) Protein Science , vol.5 , Issue.10 , pp. 2115-2118
    • Morton, C.J.1    Ladbury, J.E.2
  • 45
    • 0035816212 scopus 로고    scopus 로고
    • Specific and non-specific interactions of integration host factor with DNA: Thermodynamic evidence for disruption of multiple IHF surface salt-bridges coupled to DNA binding
    • DOI 10.1006/jmbi.2001.4768
    • J.A. Holbrook, O.V. Tsodikov, R.M. Saecker, and M.T. Record Jr. Specific and non-specific interactions of integration host factor with DNA: thermodynamic evidence for disruption of multiple IHF surface salt-bridges coupled to DNA binding J. Mol. Biol. 310 2001 379 401 (Pubitemid 32664875)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.2 , pp. 379-401
    • Holbrook, J.A.1    Tsodikov, O.V.2    Saecker, R.M.3    Record Jr., M.T.4
  • 46
    • 1042298819 scopus 로고    scopus 로고
    • Heat Capacity Effects of Water Molecules and Ions at a Protein-DNA Interface
    • DOI 10.1016/j.jmb.2003.12.061
    • S. Bergqvist, M.A. Williams, R. O'Brien, and J.E. Ladbury Heat capacity effects of water molecules and ions at a protein-DNA interface J. Mol. Biol. 336 2004 829 842 (Pubitemid 38201534)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.4 , pp. 829-842
    • Bergqvist, S.1    Williams, M.A.2    O'Brien, R.3    Ladbury, J.E.4
  • 47
    • 0028071996 scopus 로고
    • Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates
    • DOI 10.1021/bi00209a022
    • M.E. Ferrari, and T.M. Lohman Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates Biochemistry 33 1994 12896 12910 (Pubitemid 24352881)
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12896-12910
    • Ferrari, M.E.1    Lohman, T.M.2
  • 48
    • 4644342209 scopus 로고    scopus 로고
    • Thermodynamics of DNA binding and distortion by the hyperthermophile chromatin protein Sac7d
    • DOI 10.1016/j.jmb.2004.08.042, PII S0022283604010228
    • W.B. Peters, S.P. Edmondson, and J.W. Shriver Thermodynamics of DNA binding and distortion by the hyperthermophile chromatin protein Sac7d J. Mol. Biol. 343 2004 339 360 (Pubitemid 39302546)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.2 , pp. 339-360
    • Peters, W.B.1    Edmondson, S.P.2    Shriver, J.W.3
  • 49
    • 0021755212 scopus 로고
    • Escherichia coli single-stranded DNA binding protein is mobile on DNA: 1H NMR study of its interaction with oligo- and polynucleotides
    • R. Romer, U. Schomburg, G. Krauss, and G. Maass Escherichia coli single-stranded DNA binding protein is mobile on DNA: 1H NMR study of its interaction with oligo- and polynucleotides Biochemistry 23 1984 6132 6137
    • (1984) Biochemistry , vol.23 , pp. 6132-6137
    • Romer, R.1    Schomburg, U.2    Krauss, G.3    Maass, G.4
  • 50
    • 33646205283 scopus 로고    scopus 로고
    • Microsecond dynamics of protein-DNA interactions: Direct observation of the wrapping/unwrapping kinetics of single-stranded DNA around the E. coli SSB tetramer
    • S.V. Kuznetsov, A.G. Kozlov, T.M. Lohman, and A. Ansari Microsecond dynamics of protein-DNA interactions: direct observation of the wrapping/unwrapping kinetics of single-stranded DNA around the E. coli SSB tetramer J. Mol. Biol. 359 2006 55 65
    • (2006) J. Mol. Biol. , vol.359 , pp. 55-65
    • Kuznetsov, S.V.1    Kozlov, A.G.2    Lohman, T.M.3    Ansari, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.