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Chem Commun (Camb) ; 60(48): 6134-6137, 2024 Jun 11.
Article in English | MEDLINE | ID: mdl-38829522

ABSTRACT

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.


Subject(s)
Protein Disulfide-Isomerases , Protein Disulfide-Isomerases/metabolism , Protein Disulfide-Isomerases/chemistry , Oxidation-Reduction , Protein Folding , Amino Acid Motifs , Humans , Glutathione/metabolism , Glutathione/chemistry
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