Ontology highlight
ABSTRACT:
SUBMITTER: Kovermann M
PROVIDER: S-EPMC6457538 | biostudies-literature | 2019
REPOSITORIES: biostudies-literature
Kovermann Michael M Stefan Alessandra A Castaldo Anna A Caramia Sara S Hochkoeppler Alejandro A
PloS one 20190410 4
We report here on the stability and catalytic properties of the HoLaMa DNA polymerase, a Klenow sub-fragment lacking the 3'-5' exonuclease domain. HoLaMa was overexpressed in Escherichia coli, and the enzyme was purified by means of standard chromatographic techniques. High-resolution NMR experiments revealed that HoLaMa is properly folded at pH 8.0 and 20°C. In addition, urea induced a cooperative folding to unfolding transition of HoLaMa, possessing an overall thermodynamic stability and a tra ...[more]