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Highly Organized but Pliant Active Site of DNA Polymerase β: Compensatory Mechanisms in Mutant Enzymes Revealed by Dynamics Simulations and Energy Analyses
To link conformational transitions noted for DNA polymerases with kinetic results describing catalytic efficiency and fidelity, we investigate the role of key DNA polymerase β residues on subdomain motion through simulations of five single-residue mutants: Arg-283-Ala, Tyr-271-Ala, Asp-276-Val, Arg-...
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| Autori principali: | , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Biophysical Society
2004
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1304247/ https://ncbi.nlm.nih.gov/pubmed/15189842 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.103.036012 |
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