Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions: II. Salt, temperature and oligonucleotide length effects

This publication has 15 references indexed in Scilit:

• Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions
  Journal of Molecular Biology, 1989
• Negative cooperativity within individual tetramers of Escherichia coli single strand binding protein is responsible for the transition between the (SSB)35 and (SSB)56 DNA binding modes
  Biochemistry, 1988
• 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, 1988
• A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions
  Biochemistry, 1987
• Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA
  Biochemistry, 1986
• Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein
  Journal of Molecular Biology, 1986
• Kinetics of Protein-Nucleic Acid Interactions: Use of Salt Effects to Probe Mechanisms of Interactio
  Critical Reviews in Biochemistry, 1986
• Escherichia coli single-strand deoxyribonucleic acid binding protein: stability, specificity, and kinetics of complexes with oligonucleotides and deoxyribonucleic acid
  Biochemistry, 1981
• Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids
  Journal of Molecular Biology, 1981
• A semiempirical extension of polyelectrolyte theory to the treatment of oligoelectrolytes: Application to oligonucleotide helix‐coil transitions
  Biopolymers, 1978