Six Commonly Used Protein Interaction Techniques You May Need to Know

Posted by Caroline on August 29th, 2016

Proteins once in a while demonstration alone as their capacities have a tendency to be directed. protein-protein interactions (PPIs) have been studied from different perspectives: biochemistry, quantum chemistry, molecular dynamics, signal transduction, among others. This article is to give a brief introduction about six commonly used protein interaction techniques.

Yeast two-hybrid: The two-hybrid system is a genetic method that utilizes transcriptional actions as an estimation of protein-protein interaction. It has been utilized to probe into the capacity of novel proteins as far back as they were developed. Generally, co-expression of proteins for the determination and characterization of protein interactions can be accomplished with Yeast Two-Hybrid technology.

Phage display technology: Get optimal protein binding by immobilization of an antigen on magnetic beads, and screening towards a phage library. utilizing magnetic separation technology, more positives are found and the amount of false positives is kept at the very least.

Surface Plasmon Resonance (SPR): Surface Plasmon Resonance (SPR) analysis is normally utilized for the exceedingly accurate and sensitive kinetics and affinity measurement. As for SPR analysis, the ligand-of-interest is immobilized on the surface of the biosensor chip, while the analyte is injected to flow through the chip surface. Dynamic change of the SPR angle can be detected and assayed for binding affinity when interaction occurs between the ligand and the analyte.

Protein Array: As a high-throughput method, this technique is utilized to track the interactions and activities of proteins, and determining function on a large scale. Its main features is that large numbers of proteins can be tracked in parallel.

Co-Immunoprecipitation (CO-IP): Co-IP is a conventional technique generally used for protein-protein interaction identification and validation. Taking into account the specific immunological interaction between the bait protein and its antibody, co-IP has turned into an effective and reliable method for the detecting of physiological interaction between proteins.

Pull-downs: Protein pull down assay is an in vitro affinity purification technique that utilizes a bait protein to enrich proteins that interact with the bait protein. It can be utilized for confirmation of protein-protein interactions discovered by other techniques or initial screening to identify new protein-protein interactions.