Related Experiment Video
Updated: Aug 3, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Refolding of bovine threonine-neochymotrypsinogen
Abstract:
The mixed disulfide derivative of fully reduced neochymotrypsinogen was refolded at pH 9.2 and 4 degrees C with 4 mM cysteine as the disulfide interchange catalyst. The yield of regenerated neochymotrypsinogen was 25%; the corresponding yield of refolded chymotrypsinogen was 50%. The refolded neochymotrypsinogen exhibited the characteristics of the native molecule as determined from polyacrylamide gel electrophoresis and the enzymatic properties of the activated zymogen. The rate of refolding of neochymotrypsinogen was approximately the same as that found for chymotrypsinogen. These studies show that two separate fully reduced polypeptide chains were capable of refolding, associating with one another, and regenerating a native structure with full biological activity.
Related Concept Videos
Protein Folding
Protein Folding
Molecular Chaperones and Protein Folding
The...
Protein Folding Quality Check in the RER
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Bacterial Protein Maturation

