Related Experiment Video
Updated: Jun 24, 2026

Synthesizing Amino Acids Modified with Reactive Carbonyls in Silico to Assess Structural Effects Using Molecular Dynamics Simulations
Published on: April 26, 2024
Expression, purification and molecular structure modeling of thioredoxin (Trx) and thioredoxin reductase (TrxR) from
Yiping Wang1, Xiaojian Zhang, Qing Liu
1Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan, People's Republic of China.
Abstract:
The thioredoxin system consists of thioredoxin (Trx), thioredoxin reductase (TrxR) and NADPH, which plays several key roles in maintaining the redox environment of the cell. In Acidithiobacillus ferrooxidans, thioredoxin system may play important functions in the activity regulation of periplasmic proteins and energy metabolism. Here, we cloned thioredoxin (trx) and thioredoxin reductase (trxR) genes from Acidithiobacillus ferrooxidans, and expressed the genes in Escherichia coli. His-Trx and His-TrxR were purified to homogeneity with one-step Ni-NTA affinity column chromatography. Site-directed mutagenesis results confirmed that Cys33, Cys36 of thioredoxin, and Cys142, Cys145 of thioredoxin reductase were active-site residues.
Related Concept Videos
Structure and Nomenclature of Thiols and Sulfides
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

