The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived from E. coli FkpA that allows for dimerization and provides a substrate binding region, and a C-terminal thioredoxin domain derived from E. coli DsbA. Similar to DsbC, such de novo designed chimeric (hybrid) FkpA-DsbA enzymes function, as disulfide reductases, oxidases, or isomerases, and chaperones in vivo and in vitro, despite lacking similarity to DsbC-related polypeptide sequence.Board of Regents, University of Texas Syste
Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. N...
In Escherichia coli, the Dsb family of thiol-disulfide oxidoreductases catalyzes disulfide bond form...
Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the prope...
The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived fro...
textDisulfide bond formation is an essential process for the folding and biological activity of most...
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking pro...
textBacterial proteins do not contain more than one or two of disulfide bonds in their native struct...
Disclosed are methods of producing eukaryotic disulfide bond-containing polypeptides in bacterial ho...
Abstract Aims: Posttranslational formation of disulfide bonds is essential for the folding of many s...
AbstractProteins with multiple cysteine residues often require disulfide isomerization reactions bef...
textHeterologous proteins containing multiple disulfide bonds cannot fold efficiently when expresse...
AbstractProtein disulfide isomerase (PDI) exhibits both an oxido-reductase and an isomerase activity...
AbstractDisulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cy...
International audienceBackgroundDisulfide-rich proteins or DRPs are versatile bioactive compounds th...
In Escherichia coli , DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by D...
Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. N...
In Escherichia coli, the Dsb family of thiol-disulfide oxidoreductases catalyzes disulfide bond form...
Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the prope...
The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived fro...
textDisulfide bond formation is an essential process for the folding and biological activity of most...
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking pro...
textBacterial proteins do not contain more than one or two of disulfide bonds in their native struct...
Disclosed are methods of producing eukaryotic disulfide bond-containing polypeptides in bacterial ho...
Abstract Aims: Posttranslational formation of disulfide bonds is essential for the folding of many s...
AbstractProteins with multiple cysteine residues often require disulfide isomerization reactions bef...
textHeterologous proteins containing multiple disulfide bonds cannot fold efficiently when expresse...
AbstractProtein disulfide isomerase (PDI) exhibits both an oxido-reductase and an isomerase activity...
AbstractDisulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of cy...
International audienceBackgroundDisulfide-rich proteins or DRPs are versatile bioactive compounds th...
In Escherichia coli , DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by D...
Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. N...
In Escherichia coli, the Dsb family of thiol-disulfide oxidoreductases catalyzes disulfide bond form...
Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the prope...