Related Experiment Video
Updated: Sep 3, 2026

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
Estimate of Numbers of Disulfide-Bonded Protein States
1School of Life Sciences, University of Technology Sydney and Centenary Institute, University of Sydney, Sydney, NSW, Australia. p.hogg@centenary.org.au.
Abstract:
Disulfide bonds form as proteins fold in the cell and formation was assumed to be complete when the mature protein emerges. This is not the situation for many proteins that are constitutively produced as multiple partially disulfide-bonded states. For some proteins, thousands of different states are predicted assuming no dependencies on disulfide bond formation. In this chapter, probabilities for disulfide bond formation are employed to estimate the number of disulfide-bonded states. Situations where disulfide bond formation is independent of, or dependent on, the state of other bonds in the protein are considered. Estimates of the number of disulfide-bonded protein states will assist with the conceptual and experimental challenges of studying this biology.
More Related Videos
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
12:05Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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.