Motions of the Fingers Subdomain of Klentaq1 Are Fast and Not Rate Limiting: Implications for the Molecular Basis of Fidelity in DNA Polymerases

This publication has 48 references indexed in Scilit:

• Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
  Nature, 1998
• DNA Polymerase β: Structure−Fidelity Relationship from Pre-Steady-State Kinetic Analyses of All Possible Correct and Incorrect Base Pairs for Wild Type and R283A Mutant
  Biochemistry, 1997
• Slow Rate of Phosphodiester Bond Formation Accounts for the Strong Bias that Taq DNA Polymerase Shows against 2‘,3‘-Dideoxynucleotide Terminators
  Biochemistry, 1996
• Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate
  Biochemistry, 1993
• Structure of DNA Polymerase I Klenow Fragment Bound to Duplex DNA
  Science, 1993
• Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4
  Biochemistry, 1992
• The minimal kinetic mechanism for misincorporation by DNA polymerase I (Klenow fragment)
  Biochemistry, 1992
• Kinetic mechanism of DNA polymerase I(Klenow fragment): identification of a second conformational change and evaluation of the internal equilibrium constant
  Biochemistry, 1991
• Kinetic partitioning between the exonuclease and polymerase sites in DNA error correction
  Biochemistry, 1991
• A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
  Biochemistry, 1991