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Thermodynamics of the binding of Thermus aquaticus DNA polymerase to primed-template DNA

DNA binding of the Type 1 DNA polymerase from Thermus aquaticus (Taq polymerase) and its Klentaq large fragment domain have been studied as a function of temperature. Equilibrium binding assays were performed from 5 to 70°C using a fluorescence anisotropy assay and from 10 to 60°C using isothermal t...

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Bibliografske podrobnosti
izdano v:Nucleic Acids Res
Principais autores: Datta, Kausiki, LiCata, Vince J.
Format: Artigo
Jezik:Inglês
Izdano: Oxford University Press 2003
Teme:
Online dostop:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC206472/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14500822/
https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/gkg774
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