- M/EEG Preprocessing and experimental desn - UCL
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- Crystal structure of a thermostable type B DNA polymerase from
- Frontiers ERPs Differentially Reflect Automatic and
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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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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.
Crystal structure of a thermostable type B DNA polymerase from
Comparison with the mesophilic B type DNA polymerase gp43 of the bacteriophage RB69 hhts thermophilic adaptations, which include the presence of two disulfide bonds and an enhanced electrostatic complementarity at the DNA–protein interface.
Frontiers ERPs Differentially Reflect Automatic and
In contrast to gp43, several loops in the exonuclease and thumb domains are more closely packed; this apparently blocks primer binding to the exonuclease active site.
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