Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Protein-Protein Interfaces

Protein-Protein Interfaces

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

From DNA to Protein

From DNA to Protein

The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

What are Proteins?

What are Proteins?

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Context‑dependent targeting of thioredoxin reductase 1 in cancer: a mechanistic review.

Magyar onkologia·2026

Same author

Cystine C-S bond cleavage fuels cysteine production under disulfide reductase deficiency.

Nature chemical biology·2026

Same author

A katE katG double-knockout E. coli strain eliminates the risk of catalase contamination in recombinant proteins.

Applied microbiology and biotechnology·2026

Same author

Intracellular enzymatic reducing systems control receptor tyrosine kinase signaling via PTP1B.

Science advances·2026

Same author

Thioredoxin 1 Suppresses TXNIP-Driven Control of Glucose Metabolism in Human Cells.

Antioxidants & redox signaling·2026

Same author

Primary bovine embryonic fibroblasts demonstrate variable fitness following infection with highly pathogenic avian influenza H5N1 strains and are susceptible to a recently circulating human 2009 pandemic lineage H1N1 strain.

Microbiology spectrum·2026

Same journal

Tracking Synthetic Adhesins on Bacterial Surfaces with Immunofluorescence Microscopy.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Post-Selection Methods for Analyzing mRNA Display Selections and Optimization of Hits.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

High-Performance Computing in Tandem Mass Spectrometry (MS/MS) Peptide Identification.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Engineering and Adapting Disulfide-Containing Proteins to Enable Intracellular Functionality.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

AI-Driven Protein Research: From Prediction to Design.

Methods in molecular biology (Clifton, N.J.)·2026

Same journal

Methods for the In Vitro Selection of Protein and Peptide Libraries Using mRNA Display.

Methods in molecular biology (Clifton, N.J.)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jan 24, 2026

Detection of Protein Ubiquitination

Detection of Protein Ubiquitination

Published on: August 19, 2009

ProPerDP: A Protein Persulfide Detection Protocol.

Éva Dóka¹, Elias S J Arnér², Edward E Schmidt³

¹Department of Molecular Immunology and Toxicology, National Institute of Oncology, Budapest, Hungary.

Methods in Molecular Biology (Clifton, N.J.)

|June 1, 2019

Summary

This summary is machine-generated.

A new method, Protein Persulfide Detection Protocol (ProPerDP), accurately detects persulfides on cysteine residues in various biological samples. This technique prevents artifacts by alkylating thiols before cell lysis, improving reliability.

Keywords:

Biotin pulldown assay Detection method ProPerDP Protein persulfide Selective reduction

More Related Videos

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Nerve Ultrasound Protocol to Detect Dysimmune Neuropathies

Nerve Ultrasound Protocol to Detect Dysimmune Neuropathies

Published on: October 7, 2021

Related Experiment Videos

Last Updated: Jan 24, 2026

Detection of Protein Ubiquitination

Detection of Protein Ubiquitination

Published on: August 19, 2009

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Nerve Ultrasound Protocol to Detect Dysimmune Neuropathies

Nerve Ultrasound Protocol to Detect Dysimmune Neuropathies

Published on: October 7, 2021

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Protein persulfide and polysulfide modifications on cysteine residues are increasingly recognized as crucial regulatory post-translational modifications.
The labile nature of these persulfide species presents significant challenges for accurate intracellular detection.

Purpose of the Study:

To introduce a novel, highly selective method for detecting protein persulfide and polysulfide species.
To provide a reliable and accessible tool for researchers studying persulfide modifications in various biological contexts.

Main Methods:

Development of the Protein Persulfide Detection Protocol (ProPerDP), a selective method for persulfide detection.
Key innovation involves alkylating all thiol and persulfide species prior to cell lysis to prevent artifact formation.
Application of ProPerDP in isolated protein systems, blood plasma, and cell/tissue samples.

Main Results:

ProPerDP demonstrates high selectivity in detecting protein per- and polysulfide species.
The protocol is user-friendly, cost-effective, and utilizes readily available reagents.
The pre-lysis alkylation step significantly minimizes the detection of artifacts induced by cell lysis.

Conclusions:

ProPerDP offers a robust and reliable approach for studying protein persulfide modifications.
This method overcomes limitations of previous techniques by mitigating lysis-induced artifacts.
ProPerDP facilitates the accurate investigation of the regulatory roles of persulfides in biological systems.