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

DNA Microarrays

DNA Microarrays

Microarrays are high-throughput and relatively inexpensive assays that can be automated to analyze large quantities of data at a time. They are used in genome-wide studies to compare gene or protein expression under two varied conditions, such as healthy and diseased states. Microarrays consist of glass or silica slides on which probe molecules are covalently attached through surface functionalization. Most commonly, the slides are prepared through the chemisorption of silanes to silica...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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 polypeptide...

You might also read

Related Articles

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

Sort by

Same author

The Role of Value-Based Implants in Orthopedic Trauma.

The Orthopedic clinics of North America·2018

Same author

The Role of Business Education in the Orthopedic Curriculum.

The Orthopedic clinics of North America·2018

Same author

Serum proteomic assessment of the progression of fracture healing.

Journal of orthopaedic research : official publication of the Orthopaedic Research Society·2017

Same author

Correlation between RUST assessments of fracture healing to structural and biomechanical properties.

Journal of orthopaedic research : official publication of the Orthopaedic Research Society·2017

Same author

Effect of the Spiroiminodihydantoin Lesion on Nucleosome Stability and Positioning.

Biochemistry·2016

Same author

Effect of Base-Pairing Partner on the Thermodynamic Stability of the Diastereomeric Spiroiminodihydantoin Lesion.

Chemical research in toxicology·2016

Search research articles

Related Experiment Video

Updated: Jun 28, 2026

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

Identifying protein interactions with metal-modified DNA using microarray technology.

Hope E Stansfield¹, Bethany P Kulczewski, Kyle E Lybrand

¹Department of Chemistry, Biochemistry Program, Smith College, Northampton, MA 01063, USA.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry

|October 22, 2008

Summary

This summary is machine-generated.

This study shows protein microarrays can rapidly identify proteins interacting with metal-modified DNA, discovering novel interactions with cisplatin-modified DNA and high mobility group protein 1 (HMG-1).

More Related Videos

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

Related Experiment Videos

Last Updated: Jun 28, 2026

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

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

A Protein Preparation Method for the High-throughput Identification of Proteins Interacting with a Nuclear Cofactor Using LC-MS/MS Analysis

Published on: January 24, 2017

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

Area of Science:

Biochemistry
Molecular Biology
Genomics

Background:

Protein microarrays are established for protein-protein interactions.
Application to protein-DNA interactions, especially with metal modifications, is less explored.

Purpose of the Study:

To demonstrate the utility of protein microarrays for identifying protein-metal-modified DNA interactions.
To discover novel protein interactions with metal-modified DNA using high-throughput screening.

Main Methods:

Protein macroarray experiments using high mobility group protein 1 (HMG-1) and metal-modified oligonucleotides (cisplatin, chromium).
Screening commercially available human protein microarrays for interactions with cisplatin-modified DNA.

Main Results:

Proof of principle established with HMG-1 and metal-modified DNA.
Confirmed known protein-DNA interactions.
Identified numerous novel protein interactions with cisplatin-modified DNA.

Conclusions:

Protein microarrays offer a rapid, high-throughput method for discovering proteins that interact with metal-modified DNA.
This technique expands the application of microarrays to a new class of biomolecular interactions.
The findings open avenues for further research into DNA-binding proteins and metal-DNA adducts.