Triplet state properties of tryptophan residues in complexes of mutated Escherichia coli single-stranded DNA binding proteins with single-stranded polynucleotides

This publication has 20 references indexed in Scilit:

• Spin-lattice relaxation in the triplet state of the buried tryptophan residue of ribonuclease T1
  Biophysical Journal, 1986
• Strategies and Applications of in Vitro Mutagenesis
  Science, 1985
• Site-specific mutagenesis of the human fibroblast interferon gene.
  Proceedings of the National Academy of Sciences, 1984
• Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies.
  Journal of Biological Chemistry, 1984
• Close range interactions between nucleotide bases and tryptophan residues in an Escherichia coli single-stranded DNA binding protein-mercurated poly(uridylic acid) complex. A study by optically detected magnetic resonance spectroscopy.
  Journal of Biological Chemistry, 1984
• Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.
  Journal of Biological Chemistry, 1983
• Influence of the mercury blocking reagent 2-mercaptoethanol on the spectroscopic properties of complexes formed between Lys-Trp-Lys and mercurated poly(U)
  Biochemistry, 1982
• Amplification of single-strand DNA binding protein in Escherichis coli
  Nucleic Acids Research, 1980
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• The action of polynucleotide phosphorylase on 5-halogenouridine-5′ pyrophosphates
  Biochimica et Biophysica Acta, 1962