Ontology highlight
ABSTRACT:
SUBMITTER: Salsbury FR
PROVIDER: S-EPMC3383837 | biostudies-literature | 2012 Jun
REPOSITORIES: biostudies-literature
Salsbury Freddie R FR Yuan Ye Y Knaggs Michael H MH Poole Leslie B LB Fetrow Jacquelyn S JS
The journal of physical chemistry. B 20120404 23
The peroxiredoxins (Prx) are ubiquitous peroxidases involved in important biological processes; however, details of their enzymatic mechanism remain elusive. To probe potential dynamics-function relationships, molecular dynamics simulations and electrostatic calculations were performed on the atypical 2-cysteine thiol peroxidase (Tpx) from Streptococcus pneumoniae and results compared to a previous study of a typical 2-cysteine Prx from Trypanosoma cruzi. The analyses indicate a commonality betw ...[more]