Related Experiment Video
Updated: Oct 10, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Disulfide bonds are required for Serratia marcescens nuclease activity
1Department of Biochemical and Biophysical Sciences, University of Houston, TX 77204-5934.
Abstract:
The role of the two disulfide bonds found in the Serratia marcescens nuclease were tested by site directed mutagenesis and were found essential for nuclease activity, although slight residual activity remained. The requirement for disulfide bond formation may play a role in preventing the lethal action of nuclease while in the bacterial cytoplasm.
More Related Videos
11:44Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Published on: October 2, 2018
09:37Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
Published on: May 2, 2019
Related Concept Videos
Fixing Double-strand Breaks
Preparation and Reactions of Thiols
Preparation and Reactions of 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.
Single-Strand DNA Binding Proteins
Sulfur Assimilation