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Volumn 349, Issue 2, 2005, Pages 317-330

Salt dependent binding of T4 gene 32 protein to single and double-stranded DNA: Single molecule force spectroscopy measurements

Author keywords

DNA melting; DNA replication; Force spectroscopy; Single molecule; Single stranded binding protein

Indexed keywords

BACTERIOPHAGE T4 GENE 32 PROTEIN; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; SINGLE STRANDED DNA; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 18844364649     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.03.065     Document Type: Article
Times cited : (69)

References (54)
  • 1
    • 0014793184 scopus 로고
    • Function of gene 32-protein, a new protein essential for the genetic recombination and replication of T4 bacteriophage DNA
    • B.M. Alberts Function of gene 32-protein, a new protein essential for the genetic recombination and replication of T4 bacteriophage DNA Fed. Proc. Fed. Am. Soc. Expt. Biol. 29 1970 1154 1163
    • (1970) Fed. Proc. Fed. Am. Soc. Expt. Biol. , vol.29 , pp. 1154-1163
    • Alberts, B.M.1
  • 3
    • 0036280384 scopus 로고    scopus 로고
    • LAST motifs and SMART domains in gene 32 protein: An unfolding story of autoregulation?
    • R.L. Karpel LAST motifs and SMART domains in gene 32 protein: an unfolding story of autoregulation? IUBMB Life 53 2002 161 166
    • (2002) IUBMB Life , vol.53 , pp. 161-166
    • Karpel, R.L.1
  • 4
    • 0014963741 scopus 로고
    • T4 bacteriophage gene 32: A structural protein in the replication and recombination of DNA
    • B.M. Alberts, and L. Frey T4 bacteriophage gene 32: a structural protein in the replication and recombination of DNA Nature 227 1970 1313 1318
    • (1970) Nature , vol.227 , pp. 1313-1318
    • Alberts, B.M.1    Frey, L.2
  • 6
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • 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
    • (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
  • 7
    • 0019350732 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32P*III)
    • N. Lonberg, S.C. Kowalczykowski, L.S. Paul, and P.H. von Hippel Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32P*III) J. Mol. Biol. 145 1981 123 138
    • (1981) J. Mol. Biol. , vol.145 , pp. 123-138
    • Lonberg, N.1    Kowalczykowski, S.C.2    Paul, L.S.3    Von Hippel, P.H.4
  • 8
    • 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
  • 9
    • 0018118521 scopus 로고
    • Purification and physicochemical properties of limited proteolysis products of T4 helix destabilizing protein (gene 32 protein)
    • J. Hosoda, and H. Moise Purification and physicochemical properties of limited proteolysis products of T4 helix destabilizing protein (gene 32 protein) J. Biol. Chem. 253 1978 7547 7558
    • (1978) J. Biol. Chem. , vol.253 , pp. 7547-7558
    • Hosoda, J.1    Moise, H.2
  • 10
    • 0035951867 scopus 로고    scopus 로고
    • Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein
    • L. Waidner, E. Flynn, M. Wu, X. Li, and R.L. Karpel Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein J. Biol. Chem. 276 2001 2509 2516
    • (2001) J. Biol. Chem. , vol.276 , pp. 2509-2516
    • Waidner, L.1    Flynn, E.2    Wu, M.3    Li, X.4    Karpel, R.L.5
  • 11
    • 0036009140 scopus 로고    scopus 로고
    • Thermodynamics of DNA interactions from single molecule stretching experiments
    • M.C. Williams, I. Rouzina, and V.A. Bloomfield Thermodynamics of DNA interactions from single molecule stretching experiments Accts Chem. Res. 35 2002 159 166
    • (2002) Accts Chem. Res. , vol.35 , pp. 159-166
    • Williams, M.C.1    Rouzina, I.2    Bloomfield, V.A.3
  • 13
    • 0035144565 scopus 로고    scopus 로고
    • The effect of pH on the overstretching transition of dsDNA: Evidence of force-induced DNA melting
    • M.C. Williams, J.R. Wenner, I. Rouzina, and V.A. Bloomfield The effect of pH on the overstretching transition of dsDNA: evidence of force-induced DNA melting Biophys. J. 80 2001 874 881
    • (2001) Biophys. J. , vol.80 , pp. 874-881
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 14
    • 0035072057 scopus 로고    scopus 로고
    • Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching
    • M.C. Williams, J.R. Wenner, I. Rouzina, and V.A. Bloomfield Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching Biophys. J. 80 2001 1932 1939
    • (2001) Biophys. J. , vol.80 , pp. 1932-1939
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 15
    • 0035146646 scopus 로고    scopus 로고
    • Force-induced melting of the DNA double helix. 1. Thermodynamic analysis
    • I. Rouzina, and V.A. Bloomfield Force-induced melting of the DNA double helix. 1. Thermodynamic analysis Biophys. J. 80 2001 882 893
    • (2001) Biophys. J. , vol.80 , pp. 882-893
    • Rouzina, I.1    Bloomfield, V.A.2
  • 16
    • 0035144566 scopus 로고    scopus 로고
    • Force-induced melting of the DNA double helix. 2. Effect of solution conditions
    • I. Rouzina, and V.A. Bloomfield Force-induced melting of the DNA double helix. 2. Effect of solution conditions Biophys. J. 80 2001 894 900
    • (2001) Biophys. J. , vol.80 , pp. 894-900
    • Rouzina, I.1    Bloomfield, V.A.2
  • 17
    • 0344406718 scopus 로고    scopus 로고
    • Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains
    • K. Pant, R.L. Karpel, and M.C. Williams Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains J. Mol. Biol. 327 2003 571 578
    • (2003) J. Mol. Biol. , vol.327 , pp. 571-578
    • Pant, K.1    Karpel, R.L.2    Williams, M.C.3
  • 18
    • 1042298812 scopus 로고    scopus 로고
    • Mechanical measurement of single -molecule binding rates: Kinetics of DNA helix-destablization by T4 gene 32 protein
    • K. Pant, R.L. Karpel, I. Rouzina, and M.C. Williams Mechanical measurement of single -molecule binding rates: kinetics of DNA helix-destablization by T4 gene 32 protein J. Mol. Biol. 336 2004 851 870
    • (2004) J. Mol. Biol. , vol.336 , pp. 851-870
    • Pant, K.1    Karpel, R.L.2    Rouzina, I.3    Williams, M.C.4
  • 19
    • 0025884453 scopus 로고
    • Protein-protein interactions with the acidic COOH terminus of the single-stranded DNA-binding protein of the bacteriophage T4
    • K.B. Krassa, L.S. Green, and L. Gold Protein-protein interactions with the acidic COOH terminus of the single-stranded DNA-binding protein of the bacteriophage T4 Proc. Natl Acad. Sci. USA 88 1991 4010 4014
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4010-4014
    • Krassa, K.B.1    Green, L.S.2    Gold, L.3
  • 20
    • 0027424778 scopus 로고
    • Bacteriophage T4 gene 32 protein: Modulation of protein-nucleic acid and protein-protein association by structural domains
    • J.R. Casas-Finet, and R.L. Karpel Bacteriophage T4 gene 32 protein: modulation of protein-nucleic acid and protein-protein association by structural domains Biochemistry 32 1993 9735 9744
    • (1993) Biochemistry , vol.32 , pp. 9735-9744
    • Casas-Finet, J.R.1    Karpel, R.L.2
  • 21
    • 0026570506 scopus 로고
    • Structural basis for the nucleic acid binding cooperativity of bacteriophage T4 gene 32 protein: The (Lys/Arg)3(Ser/Thr)2 (LAST) motif
    • J.R. Casas-Finet, K.R. Fischer, and R.L. Karpel Structural basis for the nucleic acid binding cooperativity of bacteriophage T4 gene 32 protein: the (Lys/Arg)3(Ser/Thr)2 (LAST) motif Proc. Natl Acad. Sci. USA 89 1992 1050 1054
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 1050-1054
    • Casas-Finet, J.R.1    Fischer, K.R.2    Karpel, R.L.3
  • 22
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Y. Shamoo, A.M. Friedman, M.R. Parsons, W.H. Konigsberg, and T.A. Steitz 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
  • 24
    • 0019774929 scopus 로고
    • Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (helix destabilizing) protein with single-stranded nucleic acids. Evidence for protein translocation
    • T.M. Lohman, and S.C. Kowalczykowski Kinetics and mechanism of the association of the bacteriophage T4 gene 32 (helix destabilizing) protein with single-stranded nucleic acids. Evidence for protein translocation J. Mol. Biol. 152 1981 67 109
    • (1981) J. Mol. Biol. , vol.152 , pp. 67-109
    • Lohman, T.M.1    Kowalczykowski, S.C.2
  • 25
    • 0019349524 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA
    • J.W. Newport, N. Lonberg, S.C. Kowalczykowski, and P.H. von Hippel Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA J. Mol. Biol. 145 1981 105 121
    • (1981) J. Mol. Biol. , vol.145 , pp. 105-121
    • Newport, J.W.1    Lonberg, N.2    Kowalczykowski, S.C.3    Von Hippel, P.H.4
  • 26
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • G.S. Manning The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides Quart. Rev. Biophys. 11 1978 179 246
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 27
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts
    • M.T.J. Record, W. Zhang, and C.F. Anderson Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts Advan. Protein Chem. 51 1998 281 353
    • (1998) Advan. Protein Chem. , vol.51 , pp. 281-353
    • Record, M.T.J.1    Zhang, W.2    Anderson, C.F.3
  • 28
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • M.T. Record, T.M. Lohman, and P.L. deHaseth Ion effects on ligand-nucleic acid interactions J. Mol. Biol. 107 1976 145 158
    • (1976) J. Mol. Biol. , vol.107 , pp. 145-158
    • Record, M.T.1    Lohman, T.M.2    Dehaseth, P.L.3
  • 29
    • 0017116135 scopus 로고
    • Theoretical calculations of the helix-coil transition of DNA in the presence of large, cooperatively binding ligands
    • J.D. McGhee Theoretical calculations of the helix-coil transition of DNA in the presence of large, cooperatively binding ligands Biopolymers 15 1976 1345 1375
    • (1976) Biopolymers , vol.15 , pp. 1345-1375
    • McGhee, J.D.1
  • 31
    • 0015153612 scopus 로고
    • Statistical thermodynamics of nucleic acid melting transitions with coupled binding equilibria
    • D.M. Crothers Statistical thermodynamics of nucleic acid melting transitions with coupled binding equilibria Biopolymers 10 1971 2147 2160
    • (1971) Biopolymers , vol.10 , pp. 2147-2160
    • Crothers, D.M.1
  • 32
    • 0017125322 scopus 로고
    • DNA "melting" proteins. III. Fluorescence "mapping" of the nucleic acid binding site of bacteriophage T4 gene 32-protein
    • R.C. Kelly, and P.H. von Hippel DNA "melting" proteins. III. Fluorescence "mapping" of the nucleic acid binding site of bacteriophage T4 gene 32-protein J. Biol. Chem. 251 1976 7229 7239
    • (1976) J. Biol. Chem. , vol.251 , pp. 7229-7239
    • Kelly, R.C.1    Von Hippel, P.H.2
  • 33
    • 0017145254 scopus 로고
    • DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures
    • D.E. Jensen, R.C. Kelly, and P.H. von Hippel DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures J. Biol. Chem. 251 1976 7215 7228
    • (1976) J. Biol. Chem. , vol.251 , pp. 7215-7228
    • Jensen, D.E.1    Kelly, R.C.2    Von Hippel, P.H.3
  • 34
    • 0017125321 scopus 로고
    • DNA "melting" proteins. I. Effects of bovine pancreatic ribonuclease binding on the conformation and stability of DNA
    • D.E. Jensen, and P.H. von Hippel DNA "melting" proteins. I. Effects of bovine pancreatic ribonuclease binding on the conformation and stability of DNA J. Biol. Chem. 251 1976 7198 7214
    • (1976) J. Biol. Chem. , vol.251 , pp. 7198-7214
    • Jensen, D.E.1    Von Hippel, P.H.2
  • 35
    • 0021770892 scopus 로고
    • Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. 1. Irreversible dissociation induced by sodium chloride concentration jumps
    • T.M. Lohman Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. 1. Irreversible dissociation induced by sodium chloride concentration jumps Biochemistry 23 1984 4656 4665
    • (1984) Biochemistry , vol.23 , pp. 4656-4665
    • Lohman, T.M.1
  • 36
    • 0036106380 scopus 로고    scopus 로고
    • Salt dependence of the elasticity and overstretching transition of single DNA molecules
    • J.R. Wenner, M.C. Williams, I. Rouzina, and V.A. Bloomfield Salt dependence of the elasticity and overstretching transition of single DNA molecules Biophys. J. 82 2002 3160 3169
    • (2002) Biophys. J. , vol.82 , pp. 3160-3169
    • Wenner, J.R.1    Williams, M.C.2    Rouzina, I.3    Bloomfield, V.A.4
  • 37
    • 0023010470 scopus 로고
    • The effect of sequence heterogeneity on DNA melting kinetics
    • V.V. Anshelevich, and A.V. Vologodskii The effect of sequence heterogeneity on DNA melting kinetics J. Biomol. Struct. Dynam. 4 1986 251 262
    • (1986) J. Biomol. Struct. Dynam. , vol.4 , pp. 251-262
    • Anshelevich, V.V.1    Vologodskii, A.V.2
  • 38
    • 0021305622 scopus 로고
    • Slow relaxation processes in the melting of linear biopolymers: A theory and its application to nucleic acids
    • V.V. Anshelevich, A.V. Vologodskii, A.V. Lukashin, and M.D. Frank-Kamenetskii Slow relaxation processes in the melting of linear biopolymers: a theory and its application to nucleic acids Biopolymers 1 1984 39 58
    • (1984) Biopolymers , vol.1 , pp. 39-58
    • Anshelevich, V.V.1    Vologodskii, A.V.2    Lukashin, A.V.3    Frank-Kamenetskii, M.D.4
  • 39
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • J.D. McGhee, and P.H. von Hippel Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice J. Mol. Biol. 86 1974 469 489
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Von Hippel, P.H.2
  • 40
    • 0030932899 scopus 로고    scopus 로고
    • Competitive electrostatic binding of charged ligands to polyelectrolytes - Practical approach using the non-linear Poisson-Boltzmann equation
    • I. Rouzina, and V.A. Bloomfield Competitive electrostatic binding of charged ligands to polyelectrolytes - practical approach using the non-linear Poisson-Boltzmann equation Biophys. Chem. 64 1997 139 155
    • (1997) Biophys. Chem. , vol.64 , pp. 139-155
    • Rouzina, I.1    Bloomfield, V.A.2
  • 41
    • 0021770897 scopus 로고
    • Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. 2. Changes in mechanism as a function of sodium chloride concentration and other solution variables
    • T.M. Lohman Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. 2. Changes in mechanism as a function of sodium chloride concentration and other solution variables Biochemistry 23 1984 4665 4675
    • (1984) Biochemistry , vol.23 , pp. 4665-4675
    • Lohman, T.M.1
  • 42
    • 0025286323 scopus 로고
    • Over-expression, purification and characterization of recombinant T4 gene 32 protein22-301(g32P-B)
    • D.P. Giedroc, R. Khan, and K. Barnhart Over-expression, purification and characterization of recombinant T4 gene 32 protein22-301(g32P-B) J. Biol. Chem. 265 1990 11444 11455
    • (1990) J. Biol. Chem. , vol.265 , pp. 11444-11455
    • Giedroc, D.P.1    Khan, R.2    Barnhart, K.3
  • 43
    • 0027457508 scopus 로고
    • Assembly of the bacteriophage T4 replication machine requires the acidic carboxy terminus of gene 32 protein
    • J.M. Hurley, S.A. Chervitz, T.C. Jarvis, B.S. Singer, and L. Gold Assembly of the bacteriophage T4 replication machine requires the acidic carboxy terminus of gene 32 protein J. Mol. Biol. 229 1993 398 418
    • (1993) J. Mol. Biol. , vol.229 , pp. 398-418
    • Hurley, J.M.1    Chervitz, S.A.2    Jarvis, T.C.3    Singer, B.S.4    Gold, L.5
  • 45
    • 0027424778 scopus 로고
    • Bacteriophage T4 gene 32 protein: Modulation of protein-nuclei acid and protein-protein association by structural domains
    • J.R. Casas Finet, and R.L. Karpel Bacteriophage T4 gene 32 protein: modulation of protein-nuclei acid and protein-protein association by structural domains Biochemistry 32 1993 9735 9744
    • (1993) Biochemistry , vol.32 , pp. 9735-9744
    • Casas Finet, J.R.1    Karpel, R.L.2
  • 46
    • 0024962352 scopus 로고
    • Site-specific mutagenesis of T4 gene 32: The role of tyrosine residues in protein-nucleic acid interactions
    • Y. Shamoo, L.R. Ghosaini, K.M. Keating, K.R. Williams, J.M. Sturtevant, and W.H. Konigsberg Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions Biochemistry 28 1989 7409 7417
    • (1989) Biochemistry , vol.28 , pp. 7409-7417
    • Shamoo, Y.1    Ghosaini, L.R.2    Keating, K.M.3    Williams, K.R.4    Sturtevant, J.M.5    Konigsberg, W.H.6
  • 47
    • 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
    • M.T. Record Jr, C.F. Anderson, and T.M. Lohman 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
  • 48
    • 0012848624 scopus 로고    scopus 로고
    • Influence of ligand spatial organization on competitive electrostatic binding to DNA
    • I. Rouzina, and V.A. Bloomfield Influence of ligand spatial organization on competitive electrostatic binding to DNA J. Phys. Chem. 100 1996 4305 4313
    • (1996) J. Phys. Chem. , vol.100 , pp. 4305-4313
    • Rouzina, I.1    Bloomfield, V.A.2
  • 49
    • 0030572245 scopus 로고    scopus 로고
    • Macroion attraction due to electrostatic correlation between screening counterions. 1. Mobile surface-adsored ions and diffuse ion cloud
    • I. Rouzina, and V.A. Bloomfield Macroion attraction due to electrostatic correlation between screening counterions. 1. Mobile surface-adsored ions and diffuse ion cloud J. Phys. Chem 100 1996 9977 9989
    • (1996) J. Phys. Chem , vol.100 , pp. 9977-9989
    • Rouzina, I.1    Bloomfield, V.A.2
  • 51
    • 77953603315 scopus 로고
    • Interaction between parallel rod-like macroions
    • F. Oosawa Interaction between parallel rod-like macroions Biopolymers 6 1968 1633 1647
    • (1968) Biopolymers , vol.6 , pp. 1633-1647
    • Oosawa, F.1
  • 53
    • 0019641904 scopus 로고
    • Polyelectrolyte theory of charged-ligand binding to nucleic acids
    • M. Gueron, and G. Weisbuch Polyelectrolyte theory of charged-ligand binding to nucleic acids Biochimie 63 1981 821 825
    • (1981) Biochimie , vol.63 , pp. 821-825
    • Gueron, M.1    Weisbuch, G.2
  • 54
    • 0007425498 scopus 로고    scopus 로고
    • Competitive electrostatic binding of charged ligands to polyelectrolytes: Planar and cylindrical geometries
    • I. Rouzina, and V.A. Bloomfield Competitive electrostatic binding of charged ligands to polyelectrolytes: planar and cylindrical geometries J. Phys. Chem. 100 1996 4292 4304
    • (1996) J. Phys. Chem. , vol.100 , pp. 4292-4304
    • Rouzina, I.1    Bloomfield, V.A.2


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