Molecular Dynamics Free-Energy Simulations of the Binding Contribution to the Fidelity of T7 DNA Polymerase-Reference-Cited by-同舟云学术

Molecular Dynamics Free-Energy Simulations of the Binding Contribution to the Fidelity of T7 DNA Polymerase

Published:2002-05-14 Issue:22 Volume:106 Page:5754-5760
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Florián Jan¹,Warshel Arieh¹,Goodman Myron F.¹

Affiliation:

1. Department of Chemistry and Department of Biological SciencesHedco Molecular Biology Laboratories, University of Southern California, Los Angeles, California 90089-1062

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp020791m

Reference26 articles.

1. Estimated using the observed rate of hydrolysis of dimethyl phosphate in water3(kwat= 10-15s-1) and the catalytic rate for polymerase I4(kcat= 5 s-1) at 25 °C.

2. Spontaneous Hydrolysis of Ionized Phosphate Monoesters and Diesters and the Proficiencies of Phosphatases and Phosphodiesterases as Catalysts

3. Elementary steps in the DNA polymerase I reaction pathway

4. Comparison between DNA melting thermodynamics and DNA polymerase fidelity.

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