메뉴 건너뛰기




Volumn 278, Issue 5, 1998, Pages 999-1014

Calorimetric studies of E. coli SSB protein-single-stranded DNA interactions. Effects of monovalent salts on binding enthalpy

Author keywords

Anion binding; Cooperativity; ITC; Oligomeric proteins; Thermodynamics

Indexed keywords

BACTERIAL PROTEIN; DNA BINDING PROTEIN; FLUORIDE SODIUM; INORGANIC SALT; SINGLE STRANDED DNA; SODIUM BROMIDE; SODIUM CHLORIDE;

EID: 0032557719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1738     Document Type: Article
Times cited : (76)

References (67)
  • 1
    • 0020695728 scopus 로고
    • Fluorescence studies of the complex formation between the gene 5 protein of bacteriophage M13 and polynucleotides
    • Alma N.C.N., Harmsen B.J.M., de Jong E.A.M., Ven J., Hilbers C.W. Fluorescence studies of the complex formation between the gene 5 protein of bacteriophage M13 and polynucleotides. J. Mol. Biol. 163:1983;47-62
    • (1983) J. Mol. Biol. , vol.163 , pp. 47-62
    • Alma, N.C.N.1    Harmsen, B.J.M.2    De Jong, E.A.M.3    Ven, J.4    Hilbers, C.W.5
  • 3
    • 0016590487 scopus 로고
    • Physiochemical properties of DNA binding proteins: Gene 32 protein of T4 and E. coli unwinding protein
    • Anderson R.A., Coleman J.E. Physiochemical properties of DNA binding proteins gene 32 protein of T4 and E. coli unwinding protein. Biochemistry. 14:1975;5485-5491
    • (1975) Biochemistry , vol.14 , pp. 5485-5491
    • Anderson, R.A.1    Coleman, J.E.2
  • 4
    • 0026059557 scopus 로고
    • Calorimetric determination of cooperative interactions in high affinity binding processes
    • Bains G., Freire E. Calorimetric determination of cooperative interactions in high affinity binding processes. Anal. Biochem. 192:1991;203-206
    • (1991) Anal. Biochem. , vol.192 , pp. 203-206
    • Bains, G.1    Freire, E.2
  • 5
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin R.L. How Hofmeister ion interactions affect protein stability. Biophys. J. 71:1996;2056-2063
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 6
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev A., Pfuetzner R.A., Edwards A.M., Frappier L. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature. 385:1997;176-181
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 7
    • 0019942441 scopus 로고
    • Equilibrium dialysis studies of polyamine binding to DNA
    • Braunlin W.H., Strick T.J., Record M.T. Jr. Equilibrium dialysis studies of polyamine binding to DNA. Biopolymers. 21:1982;1301-1314
    • (1982) Biopolymers , vol.21 , pp. 1301-1314
    • Braunlin, W.H.1    Strick, T.J.2    Record Jr., M.T.3
  • 8
    • 0023040461 scopus 로고
    • E. coli single strand binding protein forms multiple, distinct complexes with single stranded DNA
    • Bujalowski W., Lohman T.M. E. 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
  • 10
    • 0024403429 scopus 로고
    • Negative cooperativity in E. coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model
    • Bujalowski W., Lohman T.M. Negative cooperativity in E. coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model. J. Mol. Biol. 207:1989;249-268
    • (1989) J. Mol. Biol. , vol.207 , pp. 249-268
    • Bujalowski, W.1    Lohman, T.M.2
  • 11
    • 0024356728 scopus 로고
    • Negative cooperativity in E. coli single strand binding protein-oligonucleotide interactions. II. Salt temperature and oligonucleotide length effects
    • Bujalowski W., Lohman T.M. Negative cooperativity in E. coli single strand binding protein-oligonucleotide interactions. II. Salt temperature and oligonucleotide length effects. J. Mol. Biol. 207:1989;269-288
    • (1989) J. Mol. Biol. , vol.207 , pp. 269-288
    • Bujalowski, W.1    Lohman, T.M.2
  • 12
    • 0026078480 scopus 로고
    • Monomer-tetramer equilibrium of the SSB-1 mutant single strand binding protein
    • Bujalowski W., Lohman T.M. Monomer-tetramer equilibrium of the SSB-1 mutant single strand binding protein. J. Biol. Chem. 266:1991;1616-1626
    • (1991) J. Biol. Chem. , vol.266 , pp. 1616-1626
    • Bujalowski, W.1    Lohman, T.M.2
  • 13
    • 0023916373 scopus 로고
    • Binding mode transitions of E. coli single strand binding protein-single stranded DNA complexes. Cation, anion, pH and binding density effects
    • Bujalowski W., Overman L.B., Lohman T.M. Binding mode transitions of E. 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
  • 14
    • 0022367174 scopus 로고
    • Specificity of bacteriophage M13 encoded gene 5 protein to DNA and RNA studied by means of fluorescence titrations
    • Bulsink H., Harmsen B.J.M., Hilbers C.W. Specificity of bacteriophage M13 encoded gene 5 protein to DNA and RNA studied by means of fluorescence titrations. J. Biomol. Struct. Dynam. 3:1985;227-247
    • (1985) J. Biomol. Struct. Dynam. , vol.3 , pp. 227-247
    • Bulsink, H.1    Harmsen, B.J.M.2    Hilbers, C.W.3
  • 15
    • 0023658388 scopus 로고
    • Tryptophan 54 and phenylalanine 60 are involved synergistically in the binding of E. coli SSB protein to single-stranded polynucleotides
    • Casas-Finet J.R., Khamis M.I., Maki A.H., Chase J.W. Tryptophan 54 and phenylalanine 60 are involved synergistically in the binding of E. coli SSB protein to single-stranded polynucleotides. FEBS Letters. 220:1987;347-352
    • (1987) FEBS Letters , vol.220 , pp. 347-352
    • Casas-Finet, J.R.1    Khamis, M.I.2    Maki, A.H.3    Chase, J.W.4
  • 16
    • 0028999046 scopus 로고
    • Sticky ions in biological systems
    • Collins K.D. Sticky ions in biological systems. Proc. Natl Acad. Sci., USA. 92:1995;5553-5557
    • (1995) Proc. Natl Acad. Sci., USA , vol.92 , pp. 5553-5557
    • Collins, K.D.1
  • 17
    • 0031029477 scopus 로고    scopus 로고
    • Charge density dependent strength of hydration and biological structure
    • Collins K.D. Charge density dependent strength of hydration and biological structure. Biophys. J. 72:1997;65-76
    • (1997) Biophys. J. , vol.72 , pp. 65-76
    • Collins, K.D.1
  • 18
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behavior of water at interfaces
    • Collins K.D., Washabaugh M.W. The Hofmeister effect and the behavior of water at interfaces. Quart. Rev. Biophys. 18:1985;323-422
    • (1985) Quart. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 19
    • 0027416687 scopus 로고
    • Multiple binding modes of the single-stranded DNA binding protein from Escherichia coli as detected by tryptophan fluorescence and site-directed mutagenesis
    • Curth U., Greipel J., Urbanke C., Maass G. Multiple binding modes of the single-stranded DNA binding protein from Escherichia coli as detected by tryptophan fluorescence and site-directed mutagenesis. Biochemistry. 32:1993;2585-2591
    • (1993) Biochemistry , vol.32 , pp. 2585-2591
    • Curth, U.1    Greipel, J.2    Urbanke, C.3    Maass, G.4
  • 20
    • 0017701075 scopus 로고
    • The nonspecific interaction of lac repressor to DNA. An association reaction driven by counterion release
    • de Haseth P.L., Lohman T.M., Record M.T. The nonspecific interaction of lac repressor to DNA. An association reaction driven by counterion release. Biochemistry. 16:1977;4783-4790
    • (1977) Biochemistry , vol.16 , pp. 4783-4790
    • De Haseth, P.L.1    Lohman, T.M.2    Record, M.T.3
  • 21
    • 0028071996 scopus 로고
    • Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates
    • Ferrari M.E., Lohman T.M. Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates. Biochemistry. 33:1994;12896-12910
    • (1994) Biochemistry , vol.33 , pp. 12896-12910
    • Ferrari, M.E.1    Lohman, T.M.2
  • 23
    • 0021646246 scopus 로고
    • SSB protein forms several different complexes with single stranded DNA, one of which is active in the assembly of stable Rec A protein-DNA filaments
    • Griffith J.D., Harris L.D., Register J. III. SSB protein forms several different complexes with single stranded DNA, one of which is active in the assembly of stable Rec A protein-DNA filaments. Cold Spring Harbor Symp. Quant. Biol. 49:1984;553-559
    • (1984) Cold Spring Harbor Symp. Quant. Biol. , vol.49 , pp. 553-559
    • Griffith, J.D.1    Harris, L.D.2    Register III, J.3
  • 24
    • 0024378717 scopus 로고
    • Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA
    • Ha J.H., Spolar R.S., Record M.T. Jr. Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. 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 Jr., M.T.3
  • 25
    • 0030606335 scopus 로고    scopus 로고
    • Thermodynamics of sequence-specific protein-DNA interactions
    • Hard T., Lundback T. Thermodynamics of sequence-specific protein-DNA interactions. Biophys. Chem. 62:1996;121-139
    • (1996) Biophys. Chem. , vol.62 , pp. 121-139
    • Hard, T.1    Lundback, T.2
  • 26
    • 34247513828 scopus 로고
    • On the understanding of the effect of salts. Second report. On regularities in the precipitating effect of salts and their relationship to their physiological behavior
    • Hofmeister F. On the understanding of the effect of salts. Second report. On regularities in the precipitating effect of salts and their relationship to their physiological behavior. Naunyn-Schmiedebergs archive fuer Experimentelle Pathologie und Pharmakologie (Leipzig). 24:1888;247-260
    • (1888) Naunyn-Schmiedebergs archive fuer Experimentelle Pathologie und Pharmakologie (Leipzig) , vol.24 , pp. 247-260
    • Hofmeister, F.1
  • 27
    • 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
  • 28
    • 0023655856 scopus 로고
    • Investigation of the role of individual tryptophan residues in the binding of E. coli single-stranded DNA binding protein to single-stranded polynucleotides
    • Khamis M.I., Casas-Finet J.R., Maki A.H., Murphy J.B., Chase J.W. Investigation of the role of individual tryptophan residues in the binding of E. coli single-stranded DNA binding protein to single-stranded polynucleotides. J. Biol. Chem. 262:1987;10938-10945
    • (1987) J. Biol. Chem. , vol.262 , pp. 10938-10945
    • Khamis, M.I.1    Casas-Finet, J.R.2    Maki, A.H.3    Murphy, J.B.4    Chase, J.W.5
  • 29
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swivelling revealed by the crystal structures of binary and ternary complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G. Major domain swivelling revealed by the crystal structures of binary and ternary complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 90:1997;635-647
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 30
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • Kowalczykowski S.C., Lonberg N., Newport J.W., von Hippel P.H. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions. J. Mol. Biol. 145:1981;75-104
    • (1981) J. Mol. Biol. , vol.145 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.H.4
  • 32
    • 0023219316 scopus 로고
    • Replacement of KCl by K glutamate dramatically enhances protein-DNA interactions in vitro
    • Leirmo S.L., Harrison C., Cayley S., Burgess R.R., Record M.T. Jr. Replacement of KCl by K glutamate dramatically enhances protein-DNA interactions in vitro. Biochemistry. 26:1987;2095-2101
    • (1987) Biochemistry , vol.26 , pp. 2095-2101
    • Leirmo, S.L.1    Harrison, C.2    Cayley, S.3    Burgess, R.R.4    Record Jr., M.T.5
  • 34
    • 0001642655 scopus 로고
    • E. coli SSB protein: Multiple binding modes and cooperativities
    • A. Revzin. Boca Raton, FL: CRC Press
    • Lohman T.M., Bujalowski W. E. coli SSB protein multiple binding modes and cooperativities. Revzin A. The Biology of Nonspecific DNA-Protein Interactions. 1990;131-170 CRC Press, Boca Raton, FL
    • (1990) The Biology of Nonspecific DNA-Protein Interactions , pp. 131-170
    • Lohman, T.M.1    Bujalowski, W.2
  • 35
    • 0028358069 scopus 로고
    • Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single stranded DNA complexes
    • Lohman T.M., Bujalowski W. Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single stranded DNA complexes. Biochemistry. 33:1994;2260-2265
    • (1994) Biochemistry , vol.33 , pp. 2260-2265
    • Lohman, T.M.1    Bujalowski, W.2
  • 36
    • 0028246888 scopus 로고
    • Escherichia coli single stranded binding protein: DNA-binding modes and cooperativities
    • Lohman T.M., Ferrari M.E. Escherichia coli single stranded binding protein 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
  • 38
    • 0021920551 scopus 로고
    • Two binding modes in E. coli single strand binding protein-single stranded DNA complexes: Modulation by NaCl concentration
    • Lohman T.M., Overman L.B. Two binding modes in E. coli single strand binding protein-single stranded DNA complexes modulation by NaCl concentration. J. Biol. Chem. 260:1985;3594-3603
    • (1985) J. Biol. Chem. , vol.260 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 39
    • 0018074213 scopus 로고
    • Analysis of ion concentration effects on the kinetics of protein-nucleic acid interactions. Application to lac repressor-operator interactions
    • Lohman T.M., de Haseth P.L., Record M.T. Analysis of ion concentration effects on the kinetics of protein-nucleic acid interactions. Application to lac repressor-operator interactions. Biophys. Chem. 8:1978;281-294
    • (1978) Biophys. Chem. , vol.8 , pp. 281-294
    • Lohman, T.M.1    De Haseth, P.L.2    Record, M.T.3
  • 40
    • 0019330787 scopus 로고
    • Pentalysine-deoxyribonucleic acid interactions: A model for the general effects of ion concentrations on the interactions of proteins with nucleic acids
    • Lohman T.M., de Haseth P.L., Record M.T. Pentalysine-deoxyribonucleic acid interactions a model for the general effects of ion concentrations on the interactions of proteins with nucleic acids. Biochemistry. 19:1980;3522-3530
    • (1980) Biochemistry , vol.19 , pp. 3522-3530
    • Lohman, T.M.1    De Haseth, P.L.2    Record, M.T.3
  • 42
    • 0022542165 scopus 로고
    • Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein
    • Lohman T.M., Overman L.B., Datta S. Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein. J. Mol. Biol. 187:1986;603-615
    • (1986) J. Mol. Biol. , vol.187 , pp. 603-615
    • Lohman, T.M.1    Overman, L.B.2    Datta, S.3
  • 43
    • 0029933128 scopus 로고    scopus 로고
    • A highly salt-dependent enthalpy change for Escherichia coli SSB protein-nucleic acid binding due to ion-protein interactions
    • Lohman T.M., Overman L.B., Ferrari M.E., Kozlov A.G. 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
  • 44
    • 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
  • 45
    • 0025264701 scopus 로고
    • Thermo dynamic extent of counterion release upon binding oligolysines to single stranded nucleic acids
    • Mascotti D.P., Lohman T.M. Thermo dynamic extent of counterion release upon binding oligolysines to single stranded nucleic acids. Proc. Natl Acad. Sci. USA. 87:1990;3142-3146
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3142-3146
    • Mascotti, D.P.1    Lohman, T.M.2
  • 46
    • 0026730188 scopus 로고
    • Thermo dynamics of single stranded RNA binding to oligolysines containing tryptophan
    • Mascotti D.P., Lohman T.M. Thermo dynamics of single stranded RNA binding to oligolysines containing tryptophan. Biochemistry. 31:1992;8932-8946
    • (1992) Biochemistry , vol.31 , pp. 8932-8946
    • Mascotti, D.P.1    Lohman, T.M.2
  • 47
    • 0027379588 scopus 로고
    • Thermo dynamics of single-stranded RNA and DNA interactions with oligolysines containing tryptophan. Effects of base composition
    • Mascotti D.P., Lohman T.M. Thermo dynamics of single-stranded RNA and DNA interactions with oligolysines containing tryptophan. Effects of base composition. Biochemistry. 32:1993;10568-10579
    • (1993) Biochemistry , vol.32 , pp. 10568-10579
    • Mascotti, D.P.1    Lohman, T.M.2
  • 48
    • 0030920231 scopus 로고    scopus 로고
    • Thermodynamics of Oligoarginines Binding to RNA and DNA
    • Mascotti D.P., Lohman T.M. Thermodynamics of Oligoarginines Binding to RNA and DNA. Biochemistry. 36:1997;7272-7279
    • (1997) Biochemistry , vol.36 , pp. 7272-7279
    • Mascotti, D.P.1    Lohman, T.M.2
  • 49
    • 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
  • 50
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer R.R., Laine P.S. The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 54:1990;342-380
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 51
    • 0028004607 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1A spliceosomal protein with an RNA hairpin
    • Oubridge C., Ito I., Evans P.R., Teo C.H., Nagai K. Crystal structure of the RNA-binding domain of the U1A spliceosomal protein with an RNA hairpin. Nature. 372:1994;432-438
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, I.2    Evans, P.R.3    Teo, C.H.4    Nagai, K.5
  • 52
    • 0028297873 scopus 로고
    • Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. E. coli SSB protein-single stranded nucleic acid equilibria
    • Overman L.B., Lohman T.M. Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. E. coli SSB protein-single stranded nucleic acid equilibria. J. Mol. Biol. 236:1994;165-178
    • (1994) J. Mol. Biol. , vol.236 , pp. 165-178
    • Overman, L.B.1    Lohman, T.M.2
  • 53
    • 0024284762 scopus 로고
    • 65 binding mode. Cation and anion effects and polynucleotide specificity
    • 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
  • 54
    • 0027421536 scopus 로고
    • Characterization of the Pf3 single-strand DNA binding protein by circular dichroism spectroscopy
    • Powell M.D., Gray D.M. Characterization of the Pf3 single-strand DNA binding protein by circular dichroism spectroscopy. Biochemistry. 32:1993;12538-12547
    • (1993) Biochemistry , vol.32 , pp. 12538-12547
    • Powell, M.D.1    Gray, D.M.2
  • 55
    • 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 Å resolution
    • Raghunathan S., Ricard C.S., Lohman T.M., Waksman G. 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 Å resolution. Proc. Natl Acad. Sci. USA. 94:1997;6652-6657
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 56
    • 0016817869 scopus 로고
    • ++ ions on the helix-coil transition of DNA
    • ++ ions on the helix-coil transition of DNA. Biopolymers. 14:1975;2137
    • (1975) Biopolymers , vol.14 , pp. 2137
    • Record Jr., M.T.1
  • 58
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record M.T. Jr, Anderson C.F., Lohman T.M. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids the roles of ion association or release, screening, and ion effects on water activity. Quart. Rev. Biophys. 11:1978;103-178
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 103-178
    • Record Jr., M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 59
    • 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
    • R.T. Sauer. New York: Academic Press, Inc
    • 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. Sauer R.T. Methods in Enzymology. 1991;291-343 Academic Press, Inc, New York
    • (1991) Methods in Enzymology , pp. 291-343
    • Record Jr., M.T.1    Ha, J.-H.2    Fisher, M.A.3
  • 60
    • 0022762738 scopus 로고
    • A specific model for the conformation of single-stranded polynucleotides in complex with the helix-destabilizing protein GP32 of bacteriophage T4
    • Scheerhagen M.A., Bokma J.T., Vlaanderen C.A., Blok J., van Grondelle R. A specific model for the conformation of single-stranded polynucleotides in complex with the helix-destabilizing protein GP32 of bacteriophage T4. Biopolymers. 25:1986;1419-1448
    • (1986) Biopolymers , vol.25 , pp. 1419-1448
    • Scheerhagen, M.A.1    Bokma, J.T.2    Vlaanderen, C.A.3    Blok, J.4    Van Grondelle, R.5
  • 61
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Shamoo Y., Friedman A.M., Parsons M.R., Konigsberg W.H., Steitz T.A. Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA. Nature. 376:1995;362-366
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 62
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R.S., Record M.T. 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.2
  • 63
    • 0023666967 scopus 로고
    • Interaction between adenovirus DNA-binding protein and single-stranded polynucleotides studied by circular dichroism and ultraviolet absorption
    • van Amerongen H., van Grondelle R., van der Vliet P.C. Interaction between adenovirus DNA-binding protein and single-stranded polynucleotides studied by circular dichroism and ultraviolet absorption. Biochemistry. 26:1987;4646-4652
    • (1987) Biochemistry , vol.26 , pp. 4646-4652
    • Van Amerongen, H.1    Van Grondelle, R.2    Van Der Vliet, P.C.3
  • 64
    • 33745503743 scopus 로고
    • Ion effects on the solution structure of biological macromolecules
    • von Hippel P.H., Schleich T. Ion effects on the solution structure of biological macromolecules. Accts Chem. Res. 2:1969;257-265
    • (1969) Accts Chem. Res. , vol.2 , pp. 257-265
    • Von Hippel, P.H.1    Schleich, T.2
  • 65
    • 0023028803 scopus 로고
    • The systematic characterization by aqueous column chromatography of solutes which affect protein stability
    • Washabaugh M.W., Collins K.D. The systematic characterization by aqueous column chromatography of solutes which affect protein stability. J. Biol. Chem. 261:1986;12477-12485
    • (1986) J. Biol. Chem. , vol.261 , pp. 12477-12485
    • Washabaugh, M.W.1    Collins, K.D.2
  • 66
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J.F., Lin L.N. Rapid measurement 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.N.4
  • 67
    • 0029864013 scopus 로고    scopus 로고
    • Large electrostatic differences in the binding thermodynamics of a cationic peptide to oligomeric and polymeric DNA
    • Zhang W., Bond J.P., Anderson C.F., Lohman T.M., Record M.T. Jr. Large electrostatic differences in the binding thermodynamics of a cationic peptide to oligomeric and polymeric DNA. Proc. Natl Acad. Sci. USA. 93:1996;2511-2516
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2511-2516
    • Zhang, W.1    Bond, J.P.2    Anderson, C.F.3    Lohman, T.M.4    Record Jr., M.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.