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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| Publié dans: | Nucleic Acids Res |
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| Auteurs principaux: | , |
| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
Oxford University Press
2003
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| Sujets: | |
| Accès en ligne: | 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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