- M/EEG Preprocessing and experimental desn - UCL
- Frontiers ERPs Differentially Reflect Automatic and
- Structural study of TTR-52 reveals the mechanism by which a
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M/EEG Preprocessing and experimental desn - UCL
A physiological role of this “closed” conformation is unknown but may represent a polymerase mode, in contrast to an editing mode with an open exonuclease site.
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Frontiers ERPs Differentially Reflect Automatic and
This archaeal B DNA polymerase structure provides a starting point for structure-based desn of polymerases or lands with applications in biotechnology and the development of antiviral or anticancer agents.
Structural study of TTR-52 reveals the mechanism by which a
Most known archaeal DNA polymerases belong to the type B family, which also includes the DNA replication polymerases of eukaryotes, but maintain hh fidelity at extreme conditions.
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We describe here the 2.5 Å resolution crystal structure of a DNA polymerase from the Archaea and identify structural features of the fold and the active site that are likely responsible for its thermostable function.
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