Magnetic resonance and kinetic studies of initiator-substrate distances on RNA polymerase from Escherichia coli

This publication has 9 references indexed in Scilit:

• A novel nuclear relaxation approach for estimating distance between enzyme- and nucleotide-bound metal ions at the catalytic site of pyruvate kinase.
  Journal of Biological Chemistry, 1977
• Magnetic resonance studies of the conformation of enzyme-bound adenylyl(3' → 5')uridine and adenosine 5'-triphosphate on RNA polymerase from Escherichia coli
  Biochemistry, 1977
• Determination of metal-metal distances in E. coli glutamine synthetase by EPR
  Biochemical and Biophysical Research Communications, 1977
• Magnetic resonance and kinetic studies of the role of the divalent cation activator of RNA polymerase from Escherichia coli
  Biochemistry, 1977
• Nuclear relaxation and gelation study of the interaction of organophosphates with human normal and sickle hemoglobins. In vitro gelation of sickle oxyhemoglobin in the presence of inositol hexaphosphate.
  Journal of Biological Chemistry, 1976
• A Comparative Study of Polydeoxyribonucleotides and Polyribonucleotides by Optical Rotatory Dispersion^*
  Biochemistry, 1966
• Some physical properties of RNA polymerase.
  Proceedings of the National Academy of Sciences, 1966
• STUDIES OF RIBONICLEIC ACID POLYMERASE FROM ESCHERICHIA COLI .4. EFFECT OF OLIGONUCLEOTIDES ON RIBONUCLEIC ACID POLYMERASE REACTION WITH SYNTHETIC POLYRIBONUCLEOTIDES AS TEMPLATES
  1965
• Statistical estimations in enzyme kinetics
  Biochemical Journal, 1961