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Boosting the enzymatic activity of CxxC motif-containing PDI family members.

Tsubura KuramochiYukino YamashitaKenta AraiShingo KanemuraTakahiro MuraokaMasaki Okumura
Published in: Chemical communications (Cambridge, England) (2024)
Compounds harboring high acidity and oxidizability of thiol groups permit tuning the redox equilibrium constants of CxxC sites of members of the protein disulphide isomerase (PDI) family and thus can be used to accelerate folding processes and increase the production of native proteins by minimal loading in comparison to glutathione.
Keyphrases
  • molecular dynamics simulations
  • single molecule
  • molecular dynamics
  • hydrogen peroxide
  • protein protein
  • amino acid
  • binding protein
  • small molecule
  • clinical evaluation