Peptide ligands specific to the oxidized form of Escherichia coli thioredoxin
نویسندگان
چکیده
منابع مشابه
Production of specific IgY antibody to the recombinant FanC protein produced in Escherichia coli
Objective(s): Enterotoxigenic Escherichia coli (ETEC) strains are one of the primary causes of diarrhea in newborn calves and in humans, pigs, and sheep. IgY technology has been identified as a promising alternative to generating a mass amount of specific antibody for use in immunotherapy and immunodiagnostics. The purpose of this study was to produce specific antibody by egg yolk antibody (IgY...
متن کاملChaperone properties of Escherichia coli thioredoxin and thioredoxin reductase.
Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/o...
متن کاملMicroscopic pKa values of Escherichia coli thioredoxin.
Thiol:disulfide oxidoreductases have a CXXC motif within their active sites. To initiate the reduction of a substrate disulfide bond, the thiolate form of the N-terminal cysteine residue (CXXC) of this motif performs a nucleophilic attack. Escherichia coli thioredoxin [Trx (CGPC)] is the best characterized thiol:disulfide oxidoreductase. Previous determinations of the active-site pKa values of ...
متن کاملAntibacterial Activity of the Peptide Microcin J25 Produced by Escherichia coli
Background and objectives: Bacteriocins are generally active antimicrobial peptides effective against bacteria closely related to the producer. Escherichia coli produce two bacteriocins: colicins and microcins. Microcin J25 (Mcc J25) is an antibacterial peptide that inhibits bacterial transcription by disrupting the nucleotide-uptake channel of bacterial RNA polymerase. The objective of this st...
متن کاملEffect of Signal Peptide on Stability and Folding of Escherichia coli Thioredoxin
The signal peptide plays a key role in targeting and membrane insertion of secretory and membrane proteins in both prokaryotes and eukaryotes. In E. coli, recombinant proteins can be targeted to the periplasmic space by fusing naturally occurring signal sequences to their N-terminus. The model protein thioredoxin was fused at its N-terminus with malE and pelB signal sequences. While WT and the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
سال: 2008
ISSN: 1570-9639
DOI: 10.1016/j.bbapap.2008.06.022